ID   MRDA_ECOLI              Reviewed;         633 AA.
AC   P0AD65; P08150;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   02-SEP-2026, entry version 145.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484, ECO:0000269|PubMed:30995398};
DE   AltName: Full=Class B penicillin-binding protein 2 {ECO:0000303|PubMed:37620344};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:1103132, ECO:0000303|PubMed:3009484, ECO:0000303|PubMed:30995398, ECO:0000303|PubMed:37620344};
DE            Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000303|PubMed:3009484};
DE            Short=PBP2 {ECO:0000303|PubMed:30995398, ECO:0000303|PubMed:37620344};
DE   AltName: Full=Transpeptidase PBP2 {ECO:0000303|PubMed:37620344};
DE            Short=TP PBP2 {ECO:0000303|PubMed:37620344};
GN   Name=mrdA {ECO:0000255|HAMAP-Rule:MF_02081,
GN   ECO:0000303|PubMed:3009484};
GN   Synonyms=pbpA {ECO:0000303|PubMed:3533535,
GN   ECO:0000303|PubMed:3894330}; OrderedLocusNames=b0635, JW0630;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RC   STRAIN=K12;
RX   PubMed=3533535; DOI=10.1111/j.1432-1033.1986.tb09961.x;
RA   Asoh S., Matsuzawa H., Ishino F., Strominger J.L., Matsuhashi M., Ohta T.;
RT   "Nucleotide sequence of the pbpA gene and characteristics of the deduced
RT   amino acid sequence of penicillin-binding protein 2 of Escherichia coli
RT   K12.";
RL   Eur. J. Biochem. 160:231-238(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 321-334 AND 633, ACTIVE SITE, PENICILLIN-BINDING, AND
RP   MUTAGENESIS OF SER-330.
RX   PubMed=3148617; DOI=10.1093/oxfordjournals.jbchem.a122556;
RA   Takasuga A., Adachi H., Ishino F., Matsuhashi M., Ohta T., Matsuzawa H.;
RT   "Identification of the penicillin-binding active site of penicillin-binding
RT   protein 2 of Escherichia coli.";
RL   J. Biochem. 104:822-826(1988).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 606-633.
RC   STRAIN=K12;
RX   PubMed=2644207; DOI=10.1128/jb.171.1.558-560.1989;
RA   Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T.;
RT   "Nucleotide sequence of the rodA gene, responsible for the rod shape of
RT   Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding
RT   protein 2, constitute the rodA operon.";
RL   J. Bacteriol. 171:558-560(1989).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC   STRAIN=K12;
RX   PubMed=1103132; DOI=10.1073/pnas.72.8.2999;
RA   Spratt B.G.;
RT   "Distinct penicillin binding proteins involved in the division, elongation,
RT   and shape of Escherichia coli K12.";
RL   Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=3894330; DOI=10.1128/jb.163.2.615-622.1985;
RA   Begg K.J., Donachie W.D.;
RT   "Cell shape and division in Escherichia coli: experiments with shape and
RT   division mutants.";
RL   J. Bacteriol. 163:615-622(1985).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=3009484; DOI=10.1016/s0021-9258(19)62717-1;
RA   Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K.,
RA   Matsuzawa H., Asoh S., Ohta T., Spratt B.G.;
RT   "Peptidoglycan synthetic activities in membranes of Escherichia coli caused
RT   by overproduction of penicillin-binding protein 2 and rodA protein.";
RL   J. Biol. Chem. 261:7024-7031(1986).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12519203; DOI=10.1046/j.1365-2958.2003.03316.x;
RA   Den Blaauwen T., Aarsman M.E., Vischer N.O., Nanninga N.;
RT   "Penicillin-binding protein PBP2 of Escherichia coli localizes
RT   preferentially in the lateral wall and at mid-cell in comparison with the
RT   old cell pole.";
RL   Mol. Microbiol. 47:539-547(2003).
RN   [12] {ECO:0007744|PDB:6G9F, ECO:0007744|PDB:6G9P, ECO:0007744|PDB:6G9S}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 52-633 AND IN COMPLEXES WITH
RP   DIAZABICYCLOOCTANE INHIBITORS AVIBACTAM AND CPD4, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, PATHWAY, AND ACTIVE SITE.
RC   STRAIN=K12 {ECO:0000303|PubMed:30995398};
RX   PubMed=30995398; DOI=10.1021/acs.jmedchem.9b00338;
RA   Levy N., Bruneau J.M., Le Rouzic E., Bonnard D., Le Strat F., Caravano A.,
RA   Chevreuil F., Barbion J., Chasset S., Ledoussal B., Moreau F., Ruff M.;
RT   "Structural Basis for E. coli Penicillin Binding Protein (PBP) 2
RT   Inhibition, a Platform for Drug Design.";
RL   J. Med. Chem. 62:4742-4754(2019).
RN   [13] {ECO:0007744|PDB:8TJ3}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF FUSION CONSTRUCT OF
RP   MRDA AND MRDB/RODA, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE,
RP   AND MUTAGENESIS OF SER-330.
RX   PubMed=37620344; DOI=10.1038/s41467-023-40483-8;
RA   Nygaard R., Graham C.L.B., Belcher Dufrisne M., Colburn J.D., Pepe J.,
RA   Hydorn M.A., Corradi S., Brown C.M., Ashraf K.U., Vickery O.N.,
RA   Briggs N.S., Deering J.J., Kloss B., Botta B., Clarke O.B., Columbus L.,
RA   Dworkin J., Stansfeld P.J., Roper D.I., Mancia F.;
RT   "Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2
RT   complex.";
RL   Nat. Commun. 14:5151-5151(2023).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall
CC       (PubMed:3009484). Responsible for the determination of the rod shape of
CC       the cell (PubMed:1103132). Is probably required for lateral
CC       peptidoglycan synthesis and maintenance of the correct diameter during
CC       lateral and centripetal growth (PubMed:12519203).
CC       {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:12519203,
CC       ECO:0000269|PubMed:3009484}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02081, ECO:0000269|PubMed:3009484,
CC         ECO:0000269|PubMed:30995398};
CC   -!- ACTIVITY REGULATION: Inhibited by mecillinam and benzylpenicillin
CC       (PubMed:1103132, PubMed:3009484). Inhibited by diazabicyclooctane
CC       (DBO)-based avibactam and CPD4, with IC(50) values of 0.59 uM and 0.01
CC       uM, respectively (PubMed:30995398). {ECO:0000269|PubMed:1103132,
CC       ECO:0000269|PubMed:3009484, ECO:0000269|PubMed:30995398}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484,
CC       ECO:0000269|PubMed:37620344, ECO:0000305|PubMed:30995398}.
CC   -!- INTERACTION:
CC       P0AD65; P02918: mrcA; NbExp=5; IntAct=EBI-1124032, EBI-1126191;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02081, ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484,
CC       ECO:0000305|PubMed:37620344}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305|PubMed:37620344}.
CC       Note=Localizes preferentially in the lateral wall and at mid-cell in
CC       comparison with the old cell pole. Localization at mid-cell is
CC       dependent on active FtsI. {ECO:0000269|PubMed:12519203}.
CC   -!- DISRUPTION PHENOTYPE: Temperature-sensitive mutants grow as normal rods
CC       at 30 degrees Celsius but grow and divide as cocci during prolonged
CC       culturing at 42 degrees Celsius. {ECO:0000269|PubMed:3894330}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305}.
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DR   EMBL; X04516; CAA28201.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40835.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73736.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35282.1; -; Genomic_DNA.
DR   EMBL; M22857; AAA24570.1; -; Genomic_DNA.
DR   PIR; C24995; ZPECP2.
DR   RefSeq; NP_415168.1; NC_000913.3.
DR   RefSeq; WP_000776191.1; NZ_CP009789.1.
DR   PDB; 6G9F; X-ray; 2.35 A; A=57-615.
DR   PDB; 6G9P; X-ray; 2.10 A; A=52-633.
DR   PDB; 6G9S; X-ray; 2.00 A; A=52-633.
DR   PDB; 8TJ3; EM; 3.20 A; C=1-633.
DR   AlphaFoldDB; P0AD65; -.
DR   MDRepo; P0AD65; -.
DR   SMR; P0AD65; -.
DR   BioGRID; 4259912; 574.
DR   ComplexPortal; CPX-5718; Elongasome complex.
DR   DIP; DIP-48190N; -.
DR   FunCoup; P0AD65; 507.
DR   IntAct; P0AD65; 6.
DR   STRING; 511145.b0635; -.
DR   ChEMBL; CHEMBL1840; -.
DR   ChEMBL; CHEMBL2354313; -.
DR   DrugBank; DB01163; Amdinocillin.
DR   DrugBank; DB01602; Bacampicillin.
DR   DrugBank; DB13028; Biapenem.
DR   DrugBank; DB00578; Carbenicillin.
DR   DrugBank; DB09319; Carindacillin.
DR   DrugBank; DB01327; Cefazolin.
DR   DrugBank; DB01413; Cefepime.
DR   DrugBank; DB00671; Cefixime.
DR   DrugBank; DB13470; Cefodizime.
DR   DrugBank; DB01328; Cefonicid.
DR   DrugBank; DB01329; Cefoperazone.
DR   DrugBank; DB13682; Cefpirome.
DR   DrugBank; DB06590; Ceftaroline fosamil.
DR   DrugBank; DB00438; Ceftazidime.
DR   DrugBank; DB01415; Ceftibuten.
DR   DrugBank; DB09050; Ceftolozane.
DR   DrugBank; DB01000; Cyclacillin.
DR   DrugBank; DB06211; Doripenem.
DR   DrugBank; DB00303; Ertapenem.
DR   DrugBank; DB01598; Imipenem.
DR   DrugBank; DB00948; Mezlocillin.
DR   DrugBank; DB09320; Procaine benzylpenicillin.
DR   DrugBank; DB16335; Sulopenem etzadroxil.
DR   DrugCentral; P0AD65; -.
DR   MEROPS; X52.001; -.
DR   TCDB; 8.A.254.1.1; the mrda/mrdb complex for synthesis and positioning of peptidoglycan (mrdab) family.
DR   jPOST; P0AD65; -.
DR   PaxDb; 511145-b0635; -.
DR   EnsemblBacteria; AAC73736; AAC73736; b0635.
DR   GeneID; 75170638; -.
DR   GeneID; 75205004; -.
DR   GeneID; 945240; -.
DR   KEGG; ecj:JW0630; -.
DR   KEGG; eco:b0635; -.
DR   KEGG; ecoc:C3026_03175; -.
DR   PATRIC; fig|1411691.4.peg.1633; -.
DR   EchoBASE; EB0601; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_2_6; -.
DR   InParanoid; P0AD65; -.
DR   OMA; WRFGGWP; -.
DR   OrthoDB; 9766847at2; -.
DR   PhylomeDB; P0AD65; -.
DR   BioCyc; EcoCyc:EG10606-MONOMER; -.
DR   BioCyc; MetaCyc:EG10606-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   PRO; PR:P0AD65; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR   GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IDA:EcoliWiki.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IMP:EcoCyc.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IMP:EcoliWiki.
DR   FunFam; 3.30.1390.30:FF:000001; Peptidoglycan D,D-transpeptidase MrdA; 1.
DR   FunFam; 3.40.710.10:FF:000004; Peptidoglycan D,D-transpeptidase MrdA; 1.
DR   FunFam; 3.90.1310.10:FF:000001; Peptidoglycan D,D-transpeptidase MrdA; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   Gene3D; 3.30.1390.30; Penicillin-binding protein 2a, domain 3; 1.
DR   HAMAP; MF_02081; MrdA_transpept; 1.
DR   InterPro; IPR050515; Beta-lactam/transpept.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR017790; Penicillin-binding_protein_2.
DR   NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR   NCBIfam; NF008061; PRK10795.1; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   PDBsum; 6G9F; -.
DR   PDBsum; 6G9P; -.
DR   PDBsum; 6G9S; -.
DR   PDBsum; 8TJ3; -.
PE   1: Evidence at protein level;
KW   3D-structure; Carboxypeptidase; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Hydrolase; Membrane; Peptidoglycan synthesis; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..633
FT                   /note="Peptidoglycan D,D-transpeptidase MrdA"
FT                   /id="PRO_0000195444"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:37620344"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02081"
FT   TOPO_DOM        43..633
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:37620344"
FT   ACT_SITE        330
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02081,
FT                   ECO:0000269|PubMed:30995398, ECO:0000269|PubMed:3148617,
FT                   ECO:0000269|PubMed:37620344"
FT   MUTAGEN         330
FT                   /note="S->A: No longer binds fluorescent penicillin mimic
FT                   bocellin."
FT                   /evidence="ECO:0000269|PubMed:37620344"
FT   MUTAGEN         330
FT                   /note="S->C: No longer binds penicillin."
FT                   /evidence="ECO:0000269|PubMed:3148617"
FT   HELIX           12..39
FT                   /evidence="ECO:0007829|PDB:8TJ3"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:8TJ3"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:8TJ3"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          78..90
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           98..109
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           113..124
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:8TJ3"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           140..149
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          156..165
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           169..172
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           184..192
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           209..213
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           215..219
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          223..229
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          235..242
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          250..253
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           256..266
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          271..277
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   TURN            278..281
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          282..290
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           295..298
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           303..310
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           320..323
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           329..332
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          352..359
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          376..378
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           380..385
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           390..410
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   TURN            411..414
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           432..439
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           442..444
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           445..451
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   TURN            452..454
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           462..473
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   TURN            474..476
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          484..487
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          489..491
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           498..500
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          507..510
FT                   /evidence="ECO:0007829|PDB:6G9F"
FT   HELIX           511..524
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           531..534
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          542..548
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          571..578
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          580..582
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          585..591
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           592..594
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   STRAND          596..598
FT                   /evidence="ECO:0007829|PDB:6G9S"
FT   HELIX           600..612
FT                   /evidence="ECO:0007829|PDB:6G9S"
SQ   SEQUENCE   633 AA;  70857 MW;  FE2305C002743AF6 CRC64;
     MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY QTRSNENRIK
     LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ TLDALRSVVD LTDDDIAAFR
     KERARSHRFT SIPVKTNLTE VQVARFAVNQ YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS
     KINDKDVERL NNDGKLANYA ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK
     EVPPQAGHDI YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG
     ISSKDYSALL NDPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT TLFDPGWWQL
     PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG IDRLSEWMGK FGYGHYTGID
     LAEERSGNMP TREWKQKRFK KPWYQGDTIP VGIGQGYWTA TPIQMSKALM ILINDGIVKV
     PHLLMSTAED GKQVPWVQPH EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK
     IAAKSGTAQV FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV
     GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH
//