ID   MOMPC_CHLTH             Reviewed;         397 AA.
AC   P08780;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Major outer membrane porin, serovar C;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1, omp1C;
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=C/TW-3;
RX   PubMed=10950788; DOI=10.1086/315778;
RA   Dean D., Suchland R.J., Stamm W.E.;
RT   "Evidence for long-term cervical persistence of Chlamydia trachomatis by
RT   omp1 genotyping.";
RL   J. Infect. Dis. 182:909-916(2000).
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; M17343; AAA23156.1; -; Genomic_DNA.
DR   EMBL; AF202455; AAG09443.1; -; Genomic_DNA.
DR   PIR; S11011; MMCWTC.
DR   AlphaFoldDB; P08780; -.
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..397
FT                   /note="Major outer membrane porin, serovar C"
FT                   /id="PRO_0000020146"
SQ   SEQUENCE   397 AA;  42893 MW;  0047BCDB108E5309 CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
     RVGYYGDFVF DRVLKTDVNK EFQMGAAPTT SDVAGLQNDP TINVARPNPA YGKHMQDAEM
     FTNAAYMALN IWDRFDVFCT LGATTGYLKG NSASFNLVGL FGTKTQSSSF NTAKLIPNTA
     LNEAVVELYI NTTFAWSVGA RAALWECGCA TLGASFQYAQ SKPKVEELNV LCNASEFTIN
     KPKGYVGAEF PLNITAGTEA ATGTKDASID YHEWQASLAL SYRLNMFTPY IGVKWSRVSF
     DADTIRIAQP KLAEAILDVT TLNRTTAGKG SVVSAGTDNE LADTMQIVSL QLNKMKSRKS
     CGIAVGTTIV DADKYAVTVE ARLIDERAAH VNAQFRF