ID   TAGA_VIBCH              Reviewed;        1002 AA.
AC   P0C6Q7; O68335; P24019; Q56595; Q9KTR9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ToxR-activated gene A lipoprotein;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=tagA; OrderedLocusNames=VC_0820;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=9501228; DOI=10.1073/pnas.95.6.3134;
RA   Karaolis D.K.R., Johnson J.A., Bailey C.C., Boedeker E.C., Kaper J.B.,
RA   Reeves P.R.;
RT   "A Vibrio cholerae pathogenicity island associated with epidemic and
RT   pandemic strains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:3134-3139(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RC   STRAIN=KP8.56;
RX   PubMed=1902210; DOI=10.1128/jb.173.9.2842-2851.1991;
RA   Parsot C.R., Mekalanos J.J.;
RT   "Expression of the Vibrio cholerae gene encoding aldehyde dehydrogenase is
RT   under control of ToxR, the cholera toxin transcriptional activator.";
RL   J. Bacteriol. 173:2842-2851(1991).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93983.1; Type=Erroneous initiation; Evidence={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; AF034434; AAC12274.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93983.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M60658; AAA03050.1; -; Unassigned_DNA.
DR   PIR; B82276; B82276.
DR   PIR; T09438; T09438.
DR   RefSeq; NP_230468.1; NC_002505.1.
DR   AlphaFoldDB; P0C6Q7; -.
DR   SMR; P0C6Q7; -.
DR   STRING; 243277.VC_0820; -.
DR   DNASU; 2614487; -.
DR   EnsemblBacteria; AAF93983; AAF93983; VC_0820.
DR   KEGG; vch:VC_0820; -.
DR   PATRIC; fig|243277.26.peg.781; -.
DR   eggNOG; ENOG502Z7RH; Bacteria.
DR   HOGENOM; CLU_008787_0_0_6; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019503; Peptidase_M66_dom.
DR   InterPro; IPR022218; TagA_dom.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF12561; TagA; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51694; PEPTIDASE_M66; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW   Metalloprotease; Palmitate; Protease; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..1002
FT                   /note="ToxR-activated gene A lipoprotein"
FT                   /id="PRO_0000018190"
FT   DOMAIN          45..139
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          282..536
FT                   /note="Peptidase M66"
FT   REGION          31..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         442
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CONFLICT        67
FT                   /note="W -> S (in Ref. 3; AAA03050)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1002 AA;  114630 MW;  5497258E19D552E9 CRC64;
     MVVRYSLLMK VSFAILIFLV GCNENATSSN DQYLTDPDIS EQTKKPSRPI IDEKNKGVTD
     TSVTIEWDKI ECEKNFSHYN VIVYRKDRIE DVITIRTRNN SVFIDDLKPN SQYSIDVSSC
     LHSACSESAK IEFITLNEID YYHTTEIEKN VYGSLEGEVR FVQTHVISPE GRKNEPEIIT
     GRDALILFKP SIKNSSSILM KIYSEDGLTS KVVMKSPSML PKTDQPIDID ENNKVVSYSN
     SYWSAEIPWN KMKSGMSLHF EDENGNLGII ESERIKFSAP SELIIQNIDL GMLYKPRGRN
     IVIKELERTA VDYFQKVPVS KLIFSDYTPI HFEKITLPNG TVYTEKSADI GGWHQGDMRE
     AVGKALVSTG INNANLGIVA SSGYSQQYNR LTNHITAHTN IGYYNNGVVV HGGSGGGGIV
     TLENTLHNEW SHELGHNYGL GHYVAGGTSH GPDTSWGWDG YYKRFIANFD WKRSPQSNIR
     PDNQEVVKPF MDKYTYLWDA MSGGYDHQNG IISRYTLHHP YVARIIQDWL KNGAVVINND
     YMVWDELKNI YVYKGTNFKV PIKKGVPVVT ILGVYDPDKI NPSQLYPPTY SNYGNIFDLE
     KPRSESSLKG WQYVKDVNYL DRVNTHWHTM LVNRKEEKIC RFSYLSPKGK KFEFLGYEDI
     ENKICTGGRS IHYLEDGKKN PIESKYNDYF LLSIDGDGEI SYVPDSTIGE SKICSLKMSG
     TVYGAGFIKG NSCRQIDGVF MNGFQWAFTL NQSGVNSTYT WSNECVLKIK DKDNNIESIS
     IPNYRIEKNQ SNKIHLNISR EKPIIDINVY CGEHELTSIK VSDNPDIKLL KGPIIVGQEH
     GYTSYEPKLP SGWFKHYDNF EPKNEINHEL GKMRVNDNDE YICRFNFSDS DREMKFVGYV
     SQLSESKYIC TGGSEIYYKK NEINIELSSK ENDFEWLSVR DKNLVGSKIE FDNNKTLCVL
     DNRSFYGAGY LDENNRCTQD RQIHWSNGKQ WLFSTYKTMT YH