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OMCB_CHLP6
ID   OMCB_CHLP6              Reviewed;         557 AA.
AC   F0T377; P23701;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Large cysteine-rich periplasmic protein omcB;
DE            Short=Large-CRP;
DE   AltName: Full=60 kDa cysteine-rich OMP;
DE   AltName: Full=60 kDa outer membrane protein;
DE   AltName: Full=Cysteine-rich outer membrane protein;
DE   Contains:
DE     RecName: Full=Large cysteine-rich periplasmic protein omcB-alpha;
DE   Contains:
DE     RecName: Full=Large cysteine-rich periplasmic protein omcB-beta;
DE   Flags: Precursor;
GN   Name=omcB; Synonyms=envB; OrderedLocusNames=CPSIT_0208, G5O_0210;
OS   Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=331636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DETECTION OF DOUBLET, AND SUBUNIT.
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=2050637; DOI=10.1128/jb.173.12.3821-3830.1991;
RA   Everett K.D.E., Hatch T.P.;
RT   "Sequence analysis and lipid modification of the cysteine-rich envelope
RT   proteins of Chlamydia psittaci 6BC.";
RL   J. Bacteriol. 173:3821-3830(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=21441521; DOI=10.1128/jb.00236-11;
RA   Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.;
RT   "Full-length de novo sequence of the Chlamydophila psittaci type strain,
RT   6BC.";
RL   J. Bacteriol. 193:2662-2663(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=21622741; DOI=10.1128/jb.05277-11;
RA   Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., Jones K.M.,
RA   Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., Myers G.S.;
RT   "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and
RT   Cal10.";
RL   J. Bacteriol. 193:4039-4040(2011).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=7532170; DOI=10.1128/jb.177.4.877-882.1995;
RA   Everett K.D.E., Hatch T.P.;
RT   "Architecture of the cell envelope of Chlamydia psittaci 6BC.";
RL   J. Bacteriol. 177:877-882(1995).
RN   [5]
RP   PROTEOLYTIC PROCESSING SITES.
RC   STRAIN=ATCC VR-125 / 6BC;
RA   Everett K.D.E.;
RL   Unpublished observations (JUL-2006).
CC   -!- FUNCTION: In elementary bodies (EBs, the infectious stage, which is
CC       able to survive outside the host cell) provides the structural
CC       integrity of the outer envelope through disulfide cross-links with the
CC       small cysteine-rich protein and the major outer membrane porin. It has
CC       been described in publications as the Sarkosyl-insoluble COMC
CC       (Chlamydia outer membrane complex), and serves as the functional
CC       equivalent of peptidoglycan.
CC   -!- SUBUNIT: Part of a disulfide cross-linked outer membrane complex (COMC)
CC       composed of the major outer membrane porin (MOMP), the small cysteine-
CC       rich protein (omcA) and the large cysteine-rich periplasmic protein
CC       (omcB). {ECO:0000269|PubMed:2050637}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:7532170}.
CC   -!- CAUTION: Was thought to be an outer membrane protein as it is part of a
CC       disulfide cross-linked complex that is insoluble in the detergent
CC       Sarkosyl. In PubMed:7532170 it was shown to likely be periplasmic.
CC       {ECO:0000305}.
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DR   EMBL; M61116; AAB61619.1; -; Genomic_DNA.
DR   EMBL; CP002549; ADZ18457.1; -; Genomic_DNA.
DR   EMBL; CP002586; AEB55213.1; -; Genomic_DNA.
DR   PIR; B39439; B39439.
DR   RefSeq; WP_013462604.1; NC_017287.1.
DR   AlphaFoldDB; F0T377; -.
DR   GeneID; 12242469; -.
DR   KEGG; chb:G5O_0210; -.
DR   KEGG; chp:CPSIT_0208; -.
DR   PATRIC; fig|331636.3.peg.196; -.
DR   HOGENOM; CLU_029611_0_0_0; -.
DR   OMA; CEAEFVS; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR003506; Chlam_OMP6.
DR   InterPro; IPR001434; DUF11.
DR   Pfam; PF03504; Chlam_OMP6; 1.
DR   Pfam; PF01345; DUF11; 2.
DR   PRINTS; PR01336; CHLAMIDIAOM6.
DR   TIGRFAMs; TIGR01451; B_ant_repeat; 1.
PE   1: Evidence at protein level;
KW   Cell shape; Disulfide bond; Periplasm; Signal.
FT   SIGNAL          1..22
FT   PROPEP          23..40
FT                   /id="PRO_0000410953"
FT   CHAIN           41..557
FT                   /note="Large cysteine-rich periplasmic protein omcB-alpha"
FT                   /id="PRO_0000410954"
FT   CHAIN           58..557
FT                   /note="Large cysteine-rich periplasmic protein omcB-beta"
FT                   /id="PRO_0000410955"
SQ   SEQUENCE   557 AA;  59787 MW;  34A43AA476ECF45B CRC64;
     MSKLIRRVVT VLALTSMASS FASGKIEAAA AESLATRFIA STENSDDNVF QATAKKVRFG
     RNKNQRQEQK HTGAFCDKEF YPCEGGQCQP VDATQESCYG KMYCVRVNDD CNVEISQSVP
     EYATVGSPYP IEILAVGKKD CVNVVITQQL PCEVEFVSSD PATTPTSDSK LIWTIDRLGQ
     GEKCKITVWV KPLKEGCCFT AATVCACPEL RSYTKCGQPA ICIKQEGPEC ACLRCPVCYK
     IEVCNTGSAI ARNVVVDNPV PDGYTHASGQ RVLSFNLGDM RPGDSKCFCV EFCPQKRGKV
     TNVATVSYCG GHKCSANVTT VVNEPCVQVN ISGADWSYVC KPVEYTIVVS NPGDLKLYDV
     VIEDTAPSGA TILEAAGAEI CCNKAVWCIK EMCPGETLQF KVVAKAQSPG KFTNQVVVKT
     NSDCGTCTSC AEVTTHWKGL AATHMCVIDT NDPICVGENT VYRICVTNRG SAEDTNVSLI
     LKFSKELQPV SSSGPTKGTI TGNTVVFDAL PKLGSKESVE FSVTLKGIAP GDARGEAILS
     SDTLTVPVAD TENTHVY
 
 
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