ID   MOMPB_CHLTH             Reviewed;         394 AA.
AC   P23421;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Major outer membrane porin, serovar B;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1B;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3040664; DOI=10.1128/jb.169.9.3879-3885.1987;
RA   Stephens R.S., Sanchez-Pescador R., Wagar E.A., Inouye C., Urdea M.S.;
RT   "Diversity of Chlamydia trachomatis major outer membrane protein genes.";
RL   J. Bacteriol. 169:3879-3885(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B/Tw-5/OT;
RA   Dean D.A.;
RT   "Sequence analysis of the major outer membrane protein gene (ompA) of
RT   Chlamydia trachomatis.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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 large cysteine-rich periplasmic
CC       protein. It has been described in publications as the Sarkosyl-
CC       insoluble COMC (Chlamydia outer membrane complex), and serves as the
CC       functional equivalent of peptidoglycan (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Permits diffusion of specific solutes through the outer
CC       membrane. {ECO:0000250}.
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).
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: It is present but some of the disulfide bonds are
CC       reduced in reticulate bodies (RBs).
CC   -!- SIMILARITY: Belongs to the chlamydial porin (CP) (TC 1.B.2) family.
CC       {ECO:0000305}.
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DR   EMBL; M17342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF304856; AAG41414.1; -; Genomic_DNA.
DR   PIR; S11010; MMCWTB.
DR   AlphaFoldDB; P23421; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR000604; Major_OMP_Chlamydia.
DR   Pfam; PF01308; Chlam_OMP; 1.
DR   PRINTS; PR01334; CHLAMIDIAOMP.
PE   2: Evidence at transcript level;
KW   Cell outer membrane; Cell shape; Disulfide bond; Ion transport; Membrane;
KW   Porin; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..22
FT   CHAIN           23..394
FT                   /note="Major outer membrane porin, serovar B"
FT                   /id="PRO_0000020145"
SQ   SEQUENCE   394 AA;  42528 MW;  C364233145A69301 CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWVDAISM
     RMGYYGDFVF DRVLKTDVNK EFQMGAKPTT TTGNAVAPST LTARENPAYG RHMQDAEMFT
     NAACMALNIW DRFDVFCTLG ASSGYLKGNS ASFNLVGLFG NNENQTKVSN GAFVPNMSLD
     QSVVELYTDT AFAWSVGARA ALWECGCATL GASFQYAQSK PKVEELNVLC NAAEFTINKP
     KGYVGKELPL DLTAGTDAAT GTKDASIDYH EWQASLALSY RLNMFTPYIG VKWSRASFDA
     DTIRIAQPKS AETIFDVTTL NPTIAGAGDV KTSAEGQLGD TMQIVSLQLN KMKSRKSCGI
     AVGTTIVDAD KYAVTVETRL IDERAAHVNA QFRF