ID   A7GN86_BACCN            Unreviewed;       865 AA.
AC   A7GN86;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   04-NOV-2026, entry version 117.
DE   RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE            EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   OrderedLocusNames=Bcer98_1272 {ECO:0000313|EMBL:ABS21594.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21594.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS21594.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V.,
RA   Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans,octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.99.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00049902};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- PATHWAY: Glycan biosynthesis. {ECO:0000256|ARBA:ARBA00060592}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000764; ABS21594.1; -; Genomic_DNA.
DR   RefSeq; WP_012093761.1; NC_009674.1.
DR   STRING; 315749.Bcer98_1272; -.
DR   PaxDb; 315749-Bcer98_1272; -.
DR   GeneID; 33896620; -.
DR   KEGG; bcy:Bcer98_1272; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_5_0_9; -.
DR   OMA; AAGPIWQ; -.
DR   OrthoDB; 9766909at2; -.
DR   CDD; cd00063; FN3; 1.
DR   FunFam; 1.10.3810.10:FF:000001; Penicillin-binding protein 1A; 1.
DR   FunFam; 3.40.710.10:FF:000020; Penicillin-binding protein 1A; 1.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR063941; Fn3_PBP1.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR036950; Transglycosylase.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF31255; Fn3_PBP1; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
DR   Proteomes; UP000002300; Chromosome.
DR   AlphaFoldDB; A7GN86; -.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002300};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          679..765
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..831
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  96175 MW;  E8DB95F647F2B1F2 CRC64;
     MSENYRSRTE RKHAKQQTKD KNKKDKPKKK GSFFKKFLVT CLLLGIVGLV AGVSAFFVIV
     KDAPKLDKAK LVNPLSTKFY DKDGNFFYEY GAEKRTAITY DQVPKVVENA FLATEDARFY
     DHHGIDFKRT GKAIMENITG GFGSQGGSTI TQQVIKNYFL TMKKTPKRKV QEWYLAYKLE
     QKYSKHEILE MYLNKINLGN RSYGVATAAQ NYYGKDLKDL KLHEAAMLAG LPQGPNIYDP
     TKKENVQRAT KRRNVVLTLM NRHNFITKQQ MEEAMAIPVT EGLLPSKEVT EMPYPAFLDA
     VVKEVEKQIP DVNIGSDGLQ IYTTLDTKAQ DYAEKILDGD LIRYPNDKFQ GSFVFMDTQT
     GEVRAVGAGR KESKSTFKGH NLATDLDRQV GSTMKPIFDY GPAIEYMQWS TYHQLNDSEY
     TYSDGTKIRN ATSSYKGDVS MREALKKSLN IPALKTAQAV GLNKSKEFSE KLGMTFKQGP
     YESAAIGSNE SSPLQVAGAY AAFGNDGIYN KPHFVKEVAF PDGKKKNFKP KEERVMKDYT
     AYMITDMLRD VVKPGSGGTG SAAYVSGVDL AGKTGTQNYD KSVIEKYDIP ADANRDSWFA
     GYTPQYTMAV WTGYENDSSE NYIGDRSTKI AQQMFKVMMG KFATDRSRFE QPSSVERING
     ELYVKGAKKD AIKQIKVDPP TGVTPSYDAG SNTITLSWSG PSDVSYAASY KANDGSSGSL
     SVKGTSATLG GVKSGVTYSF SVVAQKGTGT SSPAGVSFTV PGQNADAQKK AEEEKRKAEE
     ELKKKAEEEK RKAEEELKKK AEEEKRKAEE ELKKKAEEEK RKAEEEAKKQ QEQQQNQHPQ
     QTPPEQPTGG NGGTNGESTP QPDGQ
//