ID   MOMPP_CHLPS             Reviewed;         392 AA.
AC   Q00087;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Major outer membrane porin;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1;
OS   Chlamydia psittaci (Chlamydophila psittaci).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FPN/PRING;
RX   PubMed=8277245; DOI=10.1099/00221287-139-11-2621;
RA   Storey C., Lusher M., Yates P., Richmond S.;
RT   "Evidence for Chlamydia pneumoniae of non-human origin.";
RL   J. Gen. Microbiol. 139:2621-2626(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X61096; CAA43409.1; -; Genomic_DNA.
DR   PIR; I40859; A40371.
DR   AlphaFoldDB; Q00087; -.
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..392
FT                   /note="Major outer membrane porin"
FT                   /id="PRO_0000020143"
SQ   SEQUENCE   392 AA;  42070 MW;  88B3C5D90BBA26DB CRC64;
     MKKLLKSALL FAAAGSALSL QALPVGNPAE PSLLIDGTMW EGASGDPCDP CATWCDAISI
     RAGFYGDYVF DRILKVDVNK TISGMAAAPT AASGTASNTT VAADRSNFAY GKHLQDAEWC
     TNAAYLALNI WDRFDVFCTL GASNGYFKAS SDAFNLVGLI GLAGTDFANQ RPNVEISQGI
     VELYTDTAFS WSVGARGALW ECGCATLGAE FQYAQSNPKI EMLNVTSSPA QFMIHKPRGY
     KGTAANFPLP VAAGTATATD TKSATVKYHE WQVGLALSYR LNMLVPYIGV NWSRATFDAD
     TIRIAQPKLA SAILNLTTWN PTLLGVATTL DTSNKYADFM QIVSMQINKM KSRKACGIAV
     GATLIDADKW SITGEARLID ERAAHINAQF RF