ID   MOMPA_CHLTH             Reviewed;         396 AA.
AC   P23732;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Major outer membrane porin, serovar A;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1A;
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=SA1/OT / Serovar A;
RX   PubMed=2235504; DOI=10.1093/nar/18.20.6136;
RA   Hayes L.J., Clarke I.N.;
RT   "Nucleotide sequence of the major outer membrane protein gene of Chlamydia
RT   trachomatis strain A/SA1/OT.";
RL   Nucleic Acids Res. 18:6136-6136(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; M58938; AAA23141.1; -; Genomic_DNA.
DR   EMBL; M33635; AAA92785.1; -; Genomic_DNA.
DR   PIR; S12799; S12799.
DR   AlphaFoldDB; P23732; -.
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..396
FT                   /note="Major outer membrane porin, serovar A"
FT                   /id="PRO_0000020144"
SQ   SEQUENCE   396 AA;  42878 MW;  2F9D3B0CE2D08162 CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
     RMGYYGDFVF DRVLKTDVNK EFQMGAAPTT RDVAGLEKDP VVNVARPNPA YGKHMQDAEM
     FTNAAYMALN IWDRFDVFCT LGATTGYLKG NSASFNLVGL FGTKTQSSGF DTANIVPNTA
     LNQAVVELYT DTTFAWSVGA RAALWECGCA TLGASFQYAQ SKPKVEELNV LCNASEFTIN
     KPKGYVGAEF PLDITAGTEA ATGTKDASID YHEWQASLAL SYRLNMFTPY IGVKWSRVSF
     DADTIRIAQP KLAKPVLDTT TLNPTIAGKG TVVSSAENEL ADTMQIVSLQ LNKMKSRKSC
     GIAVGTTIVD ADKYAVTVET RLIDERAAHV NAQFRF