ID   MOMPN_CHLPN             Reviewed;         389 AA.
AC   Q07430;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Major outer membrane porin;
DE            Short=MOMP;
DE   Flags: Precursor;
GN   Name=ompA; Synonyms=omp1;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N16;
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}.
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DR   EMBL; L04982; AAA17397.1; -; Unassigned_DNA.
DR   PIR; I40739; I40739.
DR   AlphaFoldDB; Q07430; -.
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..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..389
FT                   /note="Major outer membrane porin"
FT                   /id="PRO_0000020141"
SQ   SEQUENCE   389 AA;  41628 MW;  801622F05D841967 CRC64;
     MKKLLKSALL SAAFAGSVGS LQALPVGNPS DPSLLIDGTI WEGAAGDPCD PCATWCDAIS
     LRAGFYGDYV FDRILKIDAP KTFSMGAKPT GSATANYTTA VDRPNPAYNK HLYDAEWFTN
     AGFIALNIWD RFDVFCTLGA SNGYVKGNSA AFNLVGLFGV KGTSVNANEL PNVSLSNGVI
     ELYTDTTFAW SVGARGALWE CGCATLGAEF QYAQSKPKVE ELNVICNVSQ FSLNKPKGYK
     GVAFPLPTDA GVVTAAGTKS ATINYHEWQV GASLSYRLNS LVPYIGVQWS RATFDADNIR
     IAQPKLPTAI LNLTAWNPSL LGSATAVSSS DQFSDFMQIV SCQINKFKSR KACGVTVGAT
     LVDADKWSLT AEARLINERA AHISGQFRF