ID   MOMPL_CHLTH             Reviewed;         393 AA.
AC   P19542;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Major outer membrane porin, serovar L1;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1L1;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pickett M.A., Ward M.E., Clarke I.N.;
RT   "Complete nucleotide sequence of the major outer membrane protein gene from
RT   Chlamydia trachomatis serovar L1.";
RL   FEMS Microbiol. Lett. 42:185-190(1987).
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; M36533; AAA23142.1; -; Genomic_DNA.
DR   PIR; S06259; S06259.
DR   AlphaFoldDB; P19542; -.
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..393
FT                   /note="Major outer membrane porin, serovar L1"
FT                   /id="PRO_0000020151"
SQ   SEQUENCE   393 AA;  42543 MW;  7A952839408EE2DF CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
     RMGYYGDFVF DRVLQTDVNK EFQMGAKPTA TTGNAAAPST CTARENPAYG RHMQDAEMFT
     NAAYMALNIW DRFDVFCTLG ATSGYLKGNS ASFNLVGLFG DNENQSTVKK DAVPNMSFDQ
     SVVELYTDTT FAWSVGARAA LWECGCATLG ASFQYAQSKP KVEELNVLCN AAEFTINKPK
     GYVGKEFPLD LTAGTDAATG TKDASIDYHE WQASLALSYR LNMFTPYIGV KWSRASFDAD
     TIRIAQPKLA TAIFDTTTLN PTIAGAGEVK ANAEGQLGDT MQIVSLQLNK MKSRKSCGIA
     VGTTIVDADK YAVTVETRLI DERAAHVNAQ FRF