ID   MOMPF_CHLTH             Reviewed;         395 AA.
AC   P16155;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Major outer membrane porin, serovar F;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1F;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IC-CAL3 / Serovar F;
RX   PubMed=2315025; DOI=10.1093/nar/18.4.1061;
RA   Zhang Y.-X., Morrison S.G., Caldwell H.D.;
RT   "The nucleotide sequence of major outer membrane protein gene of Chlamydia
RT   trachomatis serovar F.";
RL   Nucleic Acids Res. 18:1061-1061(1990).
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; X52080; CAA36299.1; -; Genomic_DNA.
DR   PIR; S08463; MMCWTF.
DR   RefSeq; WP_009872844.1; NZ_CSTK01000001.1.
DR   AlphaFoldDB; P16155; -.
DR   PRIDE; P16155; -.
DR   eggNOG; ENOG502ZVFZ; Bacteria.
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..395
FT                   /note="Major outer membrane porin, serovar F"
FT                   /id="PRO_0000020149"
SQ   SEQUENCE   395 AA;  42586 MW;  7F90FFDEEC264ACF CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
     RMGYYGDFVF DRVLKTDVNK EFEMGEALAG ASGNTTSTLS KLVERTNPAY GKHMQDAEMF
     TNAACMTLNI WDRFDVFCTL GATSGYLKGN SASFNLVGLF GDGVNATKPA ADSIPNVQLN
     QSVVELYTDT TFAWSVGARA ALWECGCATL GASFQYAQSK PKIEELNVLC NAAEFTINKP
     KGYVGKEFPL DLTAGTDAAT GTKDASIDYH EWQASLSLSY RLNMFTPYIG VKWSRASFDS
     DTIRIAQPRL VTPVVDITTL NPTIAGCGSV AGANTEGQIS DTMQIVSLQL NKMKSRKSCG
     IAVGTTIVDA DKYAVTVETR LIDERAAHVN AQFRF