ID SDIA_ECOLI Reviewed; 240 AA. AC P07026; P76313; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 171. DE RecName: Full=Regulatory protein SdiA; DE AltName: Full=Quorum-sensing transcriptional activator {ECO:0000305}; GN Name=sdiA; OrderedLocusNames=b1916, JW1901; 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]. RX PubMed=3515318; DOI=10.1093/nar/14.5.2301; RA Sharma S., Stark T.F., Beattie W.G., Moses R.E.; RT "Multiple control elements for the uvrC gene unit of Escherichia coli."; RL Nucleic Acids Res. 14:2301-2318(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., RA Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [3] 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 [4] 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 [5] RP FUNCTION. RX PubMed=1915297; DOI=10.1002/j.1460-2075.1991.tb04900.x; RA Wang X., de Boer P.A.J., Rothfield L.I.; RT "A factor that positively regulates cell division by activating RT transcription of the major cluster of essential cell division genes of RT Escherichia coli."; RL EMBO J. 10:3363-3372(1991). RN [6] RP FUNCTION, INDUCTION BY INDOLE, AND DISRUPTION PHENOTYPE. RC STRAIN=BW25113 {ECO:0000303|PubMed:17511876}; RX PubMed=17511876; DOI=10.1186/1471-2180-7-42; RA Lee J., Jayaraman A., Wood T.K.; RT "Indole is an inter-species biofilm signal mediated by SdiA."; RL BMC Microbiol. 7:42-42(2007). RN [7] RP ROLE IN YDIV REGULATION, REPRESSION BY GLUCOSE, AND DISRUPTION PHENOTYPE. RC STRAIN=K12 / W3110 / ZK126; RX PubMed=18560382; DOI=10.1038/cr.2008.67; RA Zhou X., Meng X., Sun B.; RT "An EAL domain protein and cyclic AMP contribute to the interaction between RT the two quorum sensing systems in Escherichia coli."; RL Cell Res. 18:937-948(2008). RN [8] RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE. RC STRAIN=BW25113 {ECO:0000303|PubMed:20126629}; RX PubMed=20126629; DOI=10.1371/journal.pone.0008946; RA Dyszel J.L., Soares J.A., Swearingen M.C., Lindsay A., Smith J.N., RA Ahmer B.M.; RT "E. coli K-12 and EHEC genes regulated by SdiA."; RL PLoS ONE 5:e8946-e8946(2010). RN [9] RP FUNCTION, ACTIVITY REGULATION, INDUCTION BY INDOLE, AND DISRUPTION RP PHENOTYPE. RC STRAIN=BA4000 {ECO:0000303|PubMed:22610437}, BW25113 RC {ECO:0000303|PubMed:22610437}, K12 / MG1655 / ATCC 47076 RC {ECO:0000303|PubMed:22610437}, and K12 / W3110 / ATCC 27325 / DSM 5911 RC {ECO:0000303|PubMed:22610437}; RX PubMed=22610437; DOI=10.1128/aem.00046-12; RA Sabag-Daigle A., Soares J.A., Smith J.N., Elmasry M.E., Ahmer B.M.; RT "The acyl homoserine lactone receptor, SdiA, of Escherichia coli and RT Salmonella enterica serovar Typhimurium does not respond to indole."; RL Appl. Environ. Microbiol. 78:5424-5431(2012). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=BW25113 {ECO:0000303|PubMed:32582066}, and SM10lambdapir RC {ECO:0000303|PubMed:32582066}; RX PubMed=32582066; DOI=10.3389/fmicb.2020.01078; RA Ma X., Zhang S., Xu Z., Li H., Xiao Q., Qiu F., Zhang W., Long Y., RA Zheng D., Huang B., Chen C., Lu Y.; RT "SdiA Improves the Acid Tolerance of E. coli by Regulating GadW and GadY RT Expression."; RL Front. Microbiol. 11:1078-1078(2020). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=38027585; DOI=10.1016/j.heliyon.2023.e21658; RA Zhang S., Shu Y., Zhang W., Xu Z., Li Y., Li S., Li Q., Xiong R., Long Y., RA Liu J., Zhang Y., Chen C., Lu Y.; RT "Quorum sensing N-acyl homoserine lactones-SdiA enhances the biofilm RT formation of E. coli by regulating sRNA CsrB expression."; RL Heliyon 9:e21658-e21658(2023). RN [12] {ECO:0007744|PDB:2AVX} RP STRUCTURE BY NMR OF 3-171 IN COMPLEX WITH AUTOINDUCER, DOMAIN, AND BINDING RP OF HOMOSERINE LACTONE DERIVATIVES. RX PubMed=16307757; DOI=10.1016/j.jmb.2005.10.041; RA Yao Y., Martinez-Yamout M.A., Dickerson T.J., Brogan A.P., Wright P.E., RA Dyson H.J.; RT "Structure of the Escherichia coli quorum sensing protein SdiA: activation RT of the folding switch by acyl homoserine lactones."; RL J. Mol. Biol. 355:262-273(2006). RN [13] {ECO:0007744|PDB:4LFU, ECO:0007744|PDB:4LGW} RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS), SUBUNIT, DOMAIN, BINDING OF RP HOMOSERINE LACTONE DERIVATIVES, AND MUTAGENESIS OF CYS-232. RX PubMed=24598739; DOI=10.1107/s1399004713032355; RA Kim T., Duong T., Wu C.A., Choi J., Lan N., Kang S.W., Lokanath N.K., RA Shin D., Hwang H.Y., Kim K.K.; RT "Structural insights into the molecular mechanism of Escherichia coli SdiA, RT a quorum-sensing receptor."; RL Acta Crystallogr. D 70:694-707(2014). CC -!- FUNCTION: Activates cell division by specifically increasing CC transcription from one of the two promoters that lie immediately CC upstream of the ftsQAZ gene cluster (PubMed:1915297). However, others CC report that expression of ftsQAZ is unaffected by the chromosomal sdiA CC gene (PubMed:20126629). Activates target genes in response to CC extracellular N-acyl homoserine lactones (AHL), also known as CC autoinducers (PubMed:18560382, PubMed:20126629, PubMed:32582066). Binds CC to regulatory elements of target genes, including ftsQ P2 and uvrY CC promoter regions; DNA-binding affinity may be controlled by redox CC environment (PubMed:24598739). Autoinducer interaction may influence CC DNA-binding affinity, varying between different promoters (By CC similarity). Activates ydiV in response to autoinducer AI-1 (Vibrio CC fischeri autoinducer, N-acyl homoserine lactone oxoC6) CC (PubMed:18560382). Plays a role in regulation of the glutamate- CC dependent acid resistance system, AR-2, probably acting by activating CC gadW and gadY expression; expression of gadW is further enhanced by AHL CC (PubMed:20126629, PubMed:32582066). Role in biofilm formation is CC controversial, differing between groups (PubMed:17511876, CC PubMed:22610437, PubMed:38027585). Involved in negatively modulating CC biofilm formation, in response to indole and also to AHL CC (PubMed:17511876). Alternatively, may be involved in positively CC modulating biofilm formation, in an AHL-dependent manner CC (PubMed:38027585). However, it is also reported that SdiA plays no role CC in biofilm formation (PubMed:22610437). Not involved in conferring CC quinolone resistance, irrespective of the presence of N-hexanoyl-DL- CC homoserine lactone (C6) or oxoC6 (PubMed:20126629). Putative endogenous CC ligand, 1-octanoyl-rac-glycerol, may act as a chemical chaperone or CC placeholder in the absence of AHLs (By similarity). CC {ECO:0000250|UniProtKB:Q8XBD0, ECO:0000269|PubMed:17511876, CC ECO:0000269|PubMed:18560382, ECO:0000269|PubMed:1915297, CC ECO:0000269|PubMed:20126629, ECO:0000269|PubMed:22610437, CC ECO:0000269|PubMed:24598739, ECO:0000269|PubMed:32582066, CC ECO:0000269|PubMed:38027585}. CC -!- ACTIVITY REGULATION: Activated by interaction with the autoinducer CC signal molecule N-(3-oxo-hexanoyl)-l-homoserine lactone (oxoC6) CC (PubMed:20126629). Indole inhibits effect of oxoC6 (PubMed:22610437). CC {ECO:0000269|PubMed:20126629, ECO:0000269|PubMed:22610437}. CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:24598739}. CC -!- INDUCTION: Repressed by glucose (PubMed:18560382). Up-regulated by CC indole in strain BW25113 (PubMed:17511876). Also reported that indole CC does not up- or down-regulate SdiA expression in strains BW25113, CC MG1655 or W3110 (PubMed:22610437). {ECO:0000269|PubMed:17511876, CC ECO:0000269|PubMed:18560382, ECO:0000269|PubMed:22610437}. CC -!- DOMAIN: Binding to the autoinducer occurs via the N-terminal 170 CC residues; as E.coli does not produce LuxI autoinducers endogenously it CC should be able to bind to a number of different AI-1 autoinducers, CC which would enable it to detect other bacteria (PubMed:16307757, CC PubMed:24598739). Capable of binding autoinducers of various acyl chain CC lengths, including N-hexanoyl-l-homoserine lactone (C6-HSL), N- CC octanoyl-l-homoserine lactone (C8-HSL) and 3-oxo-C8-HSL CC (PubMed:16307757, PubMed:24598739). {ECO:0000269|PubMed:16307757, CC ECO:0000269|PubMed:24598739}. CC -!- DISRUPTION PHENOTYPE: Deletion mutant in strain BW25113 increases CC motility about 2-fold after 24 hr at 37 degrees Celsius CC (PubMed:17511876). Increases biofilm formation in strain BW25113 about CC 6-fold after 24 hr at 37 degrees Celsius and about 3.5-fold after 24 hr CC at 30 degrees Celsius (PubMed:17511876). Mutant has no effect on CC biofilm formation in strains BW25113, MG1655 and W3110 CC (PubMed:22610437). Biofilm formation is unaffected in mutant in CC SM10lambdapir strain, but reduced in the presence of homoserine lactone CC signals (PubMed:38027585). Reduces transcription of small non-coding CC RNA CsrB in SM10lambdapir or BW25113 strains; enhanced in the presence CC of combined N-acyl homoserine lactones C4-HSL and 3-oxo-C12-HSL CC (PubMed:38027585). In the presence of indole, induction of CC transcription from a ftsQ P2 promoter reporter plasmid is decreased CC about 30% in control strain BW25113, but unaffected in the deletion CC mutant (PubMed:17511876). Does not exhibit significant changes in CC expression of the chromosomal acrAB or ftsQAZ operons CC (PubMed:20126629). Significantly reduces transcription from a CC chromosomal gadW promoter reporter gene fusion in the BW25113 strain CC and reduces endogenous gadW and gadY transcript levels in SM10lambdapir CC strain (PubMed:20126629, PubMed:32582066). Exhibits 17-fold less CC survival at pH 2.5 in BW25113 strain (PubMed:17511876). Deletion in CC either SM10lambdapir or BW25113 strains impairs growth at pH 5; rescued CC by overexpression of SdiA (PubMed:32582066). Does not exhibit CC significant change in quinolone resistance (PubMed:20126629). A double CC sdiA/ydiV deletion mutant leads to decreased cAMP levels which inhibits CC quorum sensing system 2 (PubMed:18560382). CC {ECO:0000269|PubMed:17511876, ECO:0000269|PubMed:18560382, CC ECO:0000269|PubMed:20126629, ECO:0000269|PubMed:22610437, CC ECO:0000269|PubMed:32582066, ECO:0000269|PubMed:38027585}. CC -!- MISCELLANEOUS: One type of quorum sensing (QS) commonly found in Gram- CC negative bacteria utilizes a LuxI-type enzyme to produce a signaling CC molecule of the N-acyl-homoserine lactone (AHL) family, and a CC transcription factor of the LuxR family to detect and respond to the CC AHL (Probable). However, E.coli does not encode any LuxI-type AHL CC synthases and does not synthesize AHLs (Probable). SdiA is a LuxR CC family member, able to detect the QS molecules of other bacterial CC species, a behavior known as eavesdropping (Probable). CC {ECO:0000305|PubMed:22610437}. CC -!- SIMILARITY: Belongs to the autoinducer-regulated transcriptional CC regulatory protein family. {ECO:0000305}. 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; X03691; CAA27327.1; -; Genomic_DNA. DR EMBL; U00096; AAC74983.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15736.1; -; Genomic_DNA. DR PIR; A64955; QQECU1. DR RefSeq; NP_416426.1; NC_000913.3. DR RefSeq; WP_001152715.1; NZ_CP009789.1. DR PDB; 2AVX; NMR; -; A=1-171. DR PDB; 4LFU; X-ray; 2.26 A; A=1-240. DR PDB; 4LGW; X-ray; 2.70 A; A=1-240. DR AlphaFoldDB; P07026; -. DR BMRB; P07026; -. DR SMR; P07026; -. DR BioGRID; 4259602; 212. DR BioGRID; 850778; 3. DR FunCoup; P07026; 397. DR IntAct; P07026; 8. DR STRING; 511145.b1916; -. DR ChEMBL; CHEMBL4523168; -. DR DrugBank; DB07928; N-(2-OXOTETRAHYDROFURAN-3-YL)OCTANAMIDE. DR PaxDb; 511145-b1916; -. DR EnsemblBacteria; AAC74983; AAC74983; b1916. DR GeneID; 946421; -. DR KEGG; ecj:JW1901; -. DR KEGG; eco:b1916; -. DR KEGG; ecoc:C3026_10875; -. DR PATRIC; fig|1411691.4.peg.333; -. DR EchoBASE; EB0928; -. DR eggNOG; COG2197; Bacteria. DR HOGENOM; CLU_072786_7_1_6; -. DR InParanoid; P07026; -. DR OMA; CEILQWA; -. DR OrthoDB; 9774661at2; -. DR PhylomeDB; P07026; -. DR BioCyc; EcoCyc:PD02198; -. DR EvolutionaryTrace; P07026; -. DR PRO; PR:P07026; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P07026; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IDA:EcoCyc. DR CDD; cd06170; LuxR_C_like; 1. DR FunFam; 1.10.10.10:FF:000297; DNA-binding transcriptional activator SdiA; 1. DR FunFam; 3.30.450.80:FF:000002; DNA-binding transcriptional activator SdiA; 1. DR Gene3D; 3.30.450.80; Transcription factor LuxR-like, autoinducer-binding domain; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR005143; TF_LuxR_autoind-bd_dom. DR InterPro; IPR036693; TF_LuxR_autoind-bd_dom_sf. DR InterPro; IPR000792; Tscrpt_reg_LuxR_C. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR NCBIfam; NF007561; PRK10188.1; 1. DR PANTHER; PTHR44688; DNA-BINDING TRANSCRIPTIONAL ACTIVATOR DEVR_DOSR; 1. DR PANTHER; PTHR44688:SF16; DNA-BINDING TRANSCRIPTIONAL ACTIVATOR DEVR_DOSR; 1. DR Pfam; PF03472; Autoind_bind; 1. DR Pfam; PF00196; GerE; 1. DR PRINTS; PR00038; HTHLUXR. DR SMART; SM00421; HTH_LUXR; 1. DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1. DR SUPFAM; SSF75516; Pheromone-binding domain of LuxR-like quorum-sensing transcription factors; 1. DR PROSITE; PS00622; HTH_LUXR_1; 1. DR PROSITE; PS50043; HTH_LUXR_2; 1. DR PDBsum; 2AVX; -. DR PDBsum; 4LFU; -. DR PDBsum; 4LGW; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cell cycle; Cell division; Disulfide bond; KW DNA-binding; Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..240 FT /note="Regulatory protein SdiA" FT /id="PRO_0000184187" FT DOMAIN 173..238 FT /note="HTH luxR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411" FT DNA_BIND 197..216 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411" FT BINDING 43 FT /ligand="1-octanoylglycerol" FT /ligand_id="ChEBI:CHEBI:85241" FT /evidence="ECO:0000250|UniProtKB:Q8XBD0" FT BINDING 45 FT /ligand="1-octanoylglycerol" FT /ligand_id="ChEBI:CHEBI:85241" FT /evidence="ECO:0000250|UniProtKB:Q8XBD0" FT BINDING 59 FT /ligand="1-octanoylglycerol" FT /ligand_id="ChEBI:CHEBI:85241" FT /evidence="ECO:0000250|UniProtKB:Q8XBD0" FT BINDING 59 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 63 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 67 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 71 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 80 FT /ligand="1-octanoylglycerol" FT /ligand_id="ChEBI:CHEBI:85241" FT /evidence="ECO:0000250|UniProtKB:Q8XBD0" FT BINDING 80 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 82 FT /ligand="1-octanoylglycerol" FT /ligand_id="ChEBI:CHEBI:85241" FT /evidence="ECO:0000250|UniProtKB:Q8XBD0" FT BINDING 82 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 95 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 100 FT /ligand="an N-acyl-L-homoserine lactone" FT /ligand_id="ChEBI:CHEBI:55474" FT /evidence="ECO:0007744|PDB:2AVX" FT BINDING 134 FT /ligand="1-octanoylglycerol" FT /ligand_id="ChEBI:CHEBI:85241" FT /evidence="ECO:0000250|UniProtKB:Q8XBD0" FT DISULFID 232 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:24598739" FT MUTAGEN 232 FT /note="C->S: Does not form a disulfide bond." FT /evidence="ECO:0000269|PubMed:24598739" FT CONFLICT 120..128 FT /note="TQYLMLPNR -> HSVFNAAQTG (in Ref. 1; CAA27327)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="A -> R (in Ref. 1; CAA27327)" FT /evidence="ECO:0000305" FT HELIX 6..19 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 23..36 FT /evidence="ECO:0007829|PDB:4LFU" FT STRAND 40..47 FT /evidence="ECO:0007829|PDB:4LFU" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:4LFU" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 65..73 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:4LFU" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 104..112 FT /evidence="ECO:0007829|PDB:4LFU" FT STRAND 117..124 FT /evidence="ECO:0007829|PDB:4LFU" FT STRAND 130..138 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 147..167 FT /evidence="ECO:0007829|PDB:4LFU" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 182..192 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 197..204 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 208..222 FT /evidence="ECO:0007829|PDB:4LFU" FT HELIX 227..237 FT /evidence="ECO:0007829|PDB:4LFU" SQ SEQUENCE 240 AA; 28117 MW; C04CCC50C06135C4 CRC64; MQDKDFFSWR RTMLLRFQRM ETAEEVYHEI ELQAQQLEYD YYSLCVRHPV PFTRPKVAFY TNYPEAWVSY YQAKNFLAID PVLNPENFSQ GHLMWNDDLF SEAQPLWEAA RAHGLRRGVT QYLMLPNRAL GFLSFSRCSA REIPILSDEL QLKMQLLVRE SLMALMRLND EIVMTPEMNF SKREKEILRW TAEGKTSAEI AMILSISENT VNFHQKNMQK KINAPNKTQV ACYAAATGLI //