MOMPH_CHLTH
ID MOMPH_CHLTH Reviewed; 397 AA.
AC P13467;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Major outer membrane porin, serovar H;
DE Short=MOMP;
DE Flags: Precursor;
GN Name=ompA; Synonyms=omp1H;
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=Serovar H;
RX PubMed=2813066; DOI=10.1093/nar/17.20.8366;
RA Hamilton P.T., Malinowski D.P.;
RT "Nucleotide sequence of the major outer membrane protein gene from
RT Chlamydia trachomatis serovar H.";
RL Nucleic Acids Res. 17:8366-8366(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H/UW-4;
RA Dean D.A.;
RT "Sequence analysis of the major outer membrane protein gene (ompA) of
RT Chlamydia trachomatis.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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; X16007; CAA34145.1; -; Genomic_DNA.
DR EMBL; AF304857; AAG41415.1; -; Genomic_DNA.
DR PIR; S06589; MMCWTH.
DR AlphaFoldDB; P13467; -.
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..397
FT /note="Major outer membrane porin, serovar H"
FT /id="PRO_0000020150"
SQ SEQUENCE 397 AA; 42947 MW; 478ACE3808BF37BA CRC64;
MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CATWCDAISM
RVGYYGDFVF DRVLKTDVNK EFQMGAAPTT NDAADLQNDP KTNVARPNPA YGKHMQDAEM
FTNAAYMALN IWDRFDVFCT LGATTGYLKG NSASFNLVGL FGTKTKSSDF NTAKLVPNIA
LNRAVVELYT DTTFAWSVGA RAALWECGCA TLGASFQYAQ SKPKVEELNV LCNASEFTIN
KPKGYVGAEF PLDITAGTEA ATGTKDASID YHEWQASLAL SYRLNMFTPY IGVKWSRVSF
DADTIRIAQP KLAEAILDVT TLNPTIAGKG TVVASGSDND LADTMQIVSL QLNKMKSRKS
CGIAVGTTIV DADKYAVTVE TRLIDERAAH VNAQFRF
