ID   MOMPS_CHLMR             Reviewed;         404 AA.
AC   Q46407;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Major outer membrane porin;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SFPD;
RX   PubMed=8277858; DOI=10.1093/oxfordjournals.molbev.a040079;
RA   Zhang Y.-X., Fox J.G., Ho Y., Zhang L., Stills H.F. Jr., Smith T.F.;
RT   "Comparison of the major outer-membrane protein (MOMP) gene of mouse
RT   pneumonitis (MoPn) and hamster SFPD strains of Chlamydia trachomatis with
RT   other Chlamydia strains.";
RL   Mol. Biol. Evol. 10:1327-1342(1993).
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). {ECO:0000250}.
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}.
CC   -!- CAUTION: Was originally thought to originate from Chlamydia
CC       trachomatis. {ECO:0000305|PubMed:8277858}.
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DR   EMBL; L19221; AAA16615.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46407; -.
DR   TCDB; 1.B.2.1.4; the chlamydial porin (cp) family.
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                   /evidence="ECO:0000255"
FT   CHAIN           23..404
FT                   /note="Major outer membrane porin"
FT                   /id="PRO_0000253594"
FT   REGION          85..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  43105 MW;  4974D02F2AB5094D CRC64;
     MKKLLKSVLA FAVLGSASSL HALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISL
     RLGYYGDFVF DRVLKTDVNK QFEMGPVPTT TDTDAAADIT TSTPRENPAY GKHMQDAEMF
     TNAAYMALNI WDRFDVFCTL GATSGYLKGN SASFNLVGLF GDGVANAANA IATVAADSLP
     NVSLSQAVVE LYTDTAFAWS VGARAALWEC GCATLGASFQ YAQSKPKVEE LNVLCNAAQF
     TINKPKGYVG KEFPLALTAG TDSATDTKDA SIDYHEWQAS LALSYRLNMF TPYIGVKWSR
     ASFDADTIRI AQPKLAEAIL DVTTWNPTIA GAGTIADGTG AAATANGLAD TLQIVSLQLN
     KMKSRKSCGL AIGTTIVDAD KYAVTVETRL IDERAAHVNA QFRF