ID   MOMPN_CHLTH             Reviewed;         397 AA.
AC   P23114;
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 L3;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1L3;
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=L3/404;
RX   PubMed=2060793; DOI=10.1016/0378-1119(91)90240-c;
RA   Fielder T.J., Peterson E.M., de la Maza L.M.;
RT   "Nucleotide sequence of DNA encoding the major outer membrane protein of
RT   Chlamydia trachomatis serovar L3.";
RL   Gene 101:159-160(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-136.
RX   PubMed=2139622; DOI=10.1016/0378-1119(90)90499-h;
RA   Kaul R., Duncan M.J., Guest J., Wenman W.M.;
RT   "Expression of the Chlamydia trachomatis major outer membrane protein-
RT   encoding gene in Escherichia coli: role of the 3' end in mRNA stability.";
RL   Gene 87:97-103(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; X55700; CAA39226.1; -; Genomic_DNA.
DR   PIR; JE0413; JE0413.
DR   AlphaFoldDB; P23114; -.
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:0000250"
FT   CHAIN           23..397
FT                   /note="Major outer membrane porin, serovar L3"
FT                   /id="PRO_0000020153"
SQ   SEQUENCE   397 AA;  42886 MW;  F1DDCF09535C2595 CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
     RVGYYGDFVF DRVLKTDVNK EFQMGAEPTT SDTAGLSNDP TTNVARPNPA YGKHMQDAEM
     FTNAAYMALN IWDRFDVFCT LGATTGYLKG NSASFNLVGL FGTKTQSTNF NTAKLVPNTA
     LNQAVVELYT DTTFAWSVGA RAALWECGCA TLGASFQYAQ SKPKVEELNV LCDASEFTIN
     KPKGYVGAEF PLDITAGTEA ATGTKDASID YHEWQASLAL SYRLNMFTPY IGVKWSRVSF
     DADTIRIAQP KLAEAVLDVT TLNPTIAGKG SVVASGSENE LADTMQIVSL QLNKMKSRKS
     CGIAVGTTIV DADKYAVTVE TRLIDERAAH VNAQFRF