ID   MOMP6_CHLP6             Reviewed;         402 AA.
AC   Q46203; F0T5L2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Major outer membrane porin;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1; OrderedLocusNames=CPSIT_0057, G5O_0062;
OS   Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=331636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-35.
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=1856001; DOI=10.1128/iai.59.8.2853-2855.1991;
RA   Everett K.D.E., Andersen A.A., Plaunt M., Hatch T.P.;
RT   "Cloning and sequence analysis of the major outer membrane protein gene of
RT   Chlamydia psittaci 6BC.";
RL   Infect. Immun. 59:2853-2855(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=21441521; DOI=10.1128/jb.00236-11;
RA   Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.;
RT   "Full-length de novo sequence of the Chlamydophila psittaci type strain,
RT   6BC.";
RL   J. Bacteriol. 193:2662-2663(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=21622741; DOI=10.1128/jb.05277-11;
RA   Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., Jones K.M.,
RA   Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., Myers G.S.;
RT   "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and
RT   Cal10.";
RL   J. Bacteriol. 193:4039-4040(2011).
RN   [4]
RP   SUBUNIT.
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=2050637; DOI=10.1128/jb.173.12.3821-3830.1991;
RA   Everett K.D.E., Hatch T.P.;
RT   "Sequence analysis and lipid modification of the cysteine-rich envelope
RT   proteins of Chlamydia psittaci 6BC.";
RL   J. Bacteriol. 173:3821-3830(1991).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC VR-125 / 6BC;
RX   PubMed=7532170; DOI=10.1128/jb.177.4.877-882.1995;
RA   Everett K.D.E., Hatch T.P.;
RT   "Architecture of the cell envelope of Chlamydia psittaci 6BC.";
RL   J. Bacteriol. 177:877-882(1995).
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. It is present but some of the
CC       disulfide bonds are reduced in reticulate bodies (RBs).
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). {ECO:0000269|PubMed:2050637}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:7532170};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:7532170}.
CC   -!- SIMILARITY: Belongs to the chlamydial porin (CP) (TC 1.B.2) family.
CC       {ECO:0000305}.
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DR   EMBL; X56980; CAA40300.1; -; Genomic_DNA.
DR   EMBL; CP002549; ADZ18141.1; -; Genomic_DNA.
DR   EMBL; CP002586; AEB55071.1; -; Genomic_DNA.
DR   PIR; A44565; A60341.
DR   RefSeq; WP_013747314.1; NC_017287.1.
DR   AlphaFoldDB; Q46203; -.
DR   GeneID; 12242321; -.
DR   KEGG; chb:G5O_0062; -.
DR   KEGG; chp:CPSIT_0057; -.
DR   PATRIC; fig|331636.3.peg.51; -.
DR   HOGENOM; CLU_693881_0_0_0; -.
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   1: Evidence at protein level;
KW   Cell outer membrane; Cell shape; Direct protein sequencing; Disulfide bond;
KW   Ion transport; Membrane; Porin; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:1856001"
FT   CHAIN           23..402
FT                   /note="Major outer membrane porin"
FT                   /id="PRO_0000248861"
SQ   SEQUENCE   402 AA;  43261 MW;  9889F3F39B336285 CRC64;
     MKKLLKSALL FAATGSALSL QALPVGNPAE PSLLIDGTMW EGASGDPCDP CATWCDAISI
     RAGYYGDYVF DRVLKVDVNK TFSGMAATPT QATGNASNTN QPEANGRPNI AYGRHMQDAE
     WFSNAAFLAL NIWDRFDIFC TLGASNGYFK ASSAAFNLVG LIGFSAASSI STDLPMQLPN
     VGITQGVVEF YTDTSFSWSV GARGALWECG CATLGAEFQY AQSNPKIEML NVTSSPAQFV
     IHKPRGYKGA SSNFPLPITA GTTEATDTKS ATIKYHEWQV GLALSYRLNM LVPYIGVNWS
     RATFDADTIR IAQPKLKSEI LNITTWNPSL IGSTTALPNN SGKDVLSDVL QIASIQINKM
     KSRKACGVAV GATLIDADKW SITGEARLIN ERAAHMNAQF RF