ID   MOMPD_CHLTR             Reviewed;         393 AA.
AC   Q46409;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Major outer membrane porin, serovar D;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1; OrderedLocusNames=CT_681;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D/B-120;
RX   PubMed=1398119; DOI=10.1016/0378-1119(92)90022-h;
RA   Sayada C., Denamur E., Elion J.;
RT   "Complete sequence of the major outer membrane protein-encoding gene of
RT   Chlamydia trachomatis serovar Da.";
RL   Gene 120:129-130(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D/IU-71960;
RX   PubMed=9673241; DOI=10.1128/iai.66.8.3618-3625.1998;
RA   Stothard D.R., Boguslawski G., Jones R.B.;
RT   "Phylogenetic analysis of the Chlamydia trachomatis major outer membrane
RT   protein and examination of potential pathogenic determinants.";
RL   Infect. Immun. 66:3618-3625(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; X62918; CAA44701.1; -; Genomic_DNA.
DR   EMBL; AF063195; AAC31436.2; -; Genomic_DNA.
DR   EMBL; AE001273; AAC68276.1; -; Genomic_DNA.
DR   PIR; H71484; H71484.
DR   RefSeq; NP_220200.1; NC_000117.1.
DR   RefSeq; WP_010725300.1; NC_000117.1.
DR   AlphaFoldDB; Q46409; -.
DR   STRING; 272561.CT_681; -.
DR   PRIDE; Q46409; -.
DR   EnsemblBacteria; AAC68276; AAC68276; CT_681.
DR   GeneID; 884473; -.
DR   KEGG; ctr:CT_681; -.
DR   PATRIC; fig|272561.5.peg.748; -.
DR   HOGENOM; CLU_693881_0_0_0; -.
DR   OMA; SGDPCDP; -.
DR   Proteomes; UP000000431; Chromosome.
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; Reference proteome; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..393
FT                   /note="Major outer membrane porin, serovar D"
FT                   /id="PRO_0000020147"
SQ   SEQUENCE   393 AA;  42438 MW;  8CD692FD3EFF21D6 CRC64;
     MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CATWCDAISM
     RVGYYGDFVF DRVLKTDVNK EFQMGAKPTT DTGNSAAPST LTARENPAYG RHMQDAEMFT
     NAACMALNIW DRFDVFCTLG ATSGYLKGNS ASFNLVGLFG DNENQKTVKA ESVPNMSFDQ
     SVVELYTDTT FAWSVGARAA LWECGCATLG ASFQYAQSKP KVEELNVLCN AAEFTINKPK
     GYVGKEFPLD LTAGTDAATG TKDASIDYHE WQASLALSYR LNMFTPYIGV KWSRASFDAD
     TIRIAQPKSA TAIFDTTTLN PTIAGAGDVK TGAEGQLGDT MQIVSLQLNK MKSRKSCGIA
     VGTTIVDADK YAVTVETRLI DERAAHVNAQ FRF