ID   MOMPE_CHLTH             Reviewed;         393 AA.
AC   P17451;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Major outer membrane porin, serovar E;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1E;
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=BOUR / Serovar E;
RX   PubMed=2356137; DOI=10.1093/nar/18.11.3414;
RA   Peterson E.M., Markoff B.A., de la Maza L.M.;
RT   "The major outer membrane protein nucleotide sequence of Chlamydia
RT   trachomatis, serovar E.";
RL   Nucleic Acids Res. 18:3414-3414(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; X52557; CAA36791.1; -; Genomic_DNA.
DR   PIR; S10201; MMCWTE.
DR   RefSeq; WP_014541299.1; NZ_JPNI01000003.1.
DR   AlphaFoldDB; P17451; -.
DR   OMA; SGDPCDP; -.
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 E"
FT                   /id="PRO_0000020148"
SQ   SEQUENCE   393 AA;  42424 MW;  AB2B82D16027B361 CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
     RMGYYGDFVF DRVLKTDVNK EFQMGDKPTS TTGNATAPTT LTARENPAYG RHMQDAEMFT
     NAACMALNIW DRFDVFCTLG ASSGYLKGNS ASFNLVGLFG DNENQSTVKT NSVPNMSLDQ
     SVVELYTDTA FSWSVGARAA LWECGCATLG ASFQYAQSKP KVEELNVLCN AAEFTINKPK
     GYVGQEFPLA LIAGTDAATG TKDASIDYHE WQASLALSYR LNMFTPYIGV KWSRASFDAD
     TIRIAQPKSA TAIFDTTTLN PTIAGAGDVK ASAEGQLGDT MQIVSLQLNK MKSRKSCGIA
     VGTTIVDADK YAVTVETRLI DERAAHVNAQ FRF