MOMPM_CHLMU
ID MOMPM_CHLMU Reviewed; 387 AA.
AC P75024; Q04063; Q9R635; Q9X718;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Major outer membrane porin;
DE Short=MOMP;
DE Flags: Precursor;
GN Name=ompA; Synonyms=omp1; OrderedLocusNames=TC_0052;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MoPn;
RX PubMed=1937036; DOI=10.1016/0378-1119(91)90579-z;
RA Fielder T.J., Pal S., Peterson E.M., de la Maza L.M.;
RT "Sequence of the gene encoding the major outer membrane protein of the
RT mouse pneumonitis biovar of Chlamydia trachomatis.";
RL Gene 106:137-138(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MoPn;
RX PubMed=8277858; DOI=10.1093/oxfordjournals.molbev.a040079;
RA Zhang Y.-X., Fox J.G., Ho Y., Zhang L., Stills H.F. Jr., Smith T.F.;
RT "Comparison of the major outer-membrane protein (MOMP) gene of mouse
RT pneumonitis (MoPn) and hamster SFPD strains of Chlamydia trachomatis with
RT other Chlamydia strains.";
RL Mol. Biol. Evol. 10:1327-1342(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MoPn / Nigg II;
RA Carter M.W., Giles I., Everson J.S., Clarke I.N.;
RT "Chlamydia trachomatis mouse biovar: major outer membrane protein gene.";
RL (In) Mardh P.A., la Placa M., Ward M. (eds.);
RL Proceedings of the European society for chlamydia research and the second
RL international symposium of Uppsala university centre for std research,
RL pp.38-38, University of Uppsala, Uppsala (1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-375.
RC STRAIN=MoPn;
RX PubMed=8419295; DOI=10.1128/jb.175.2.487-502.1993;
RA Kaltenboeck B., Kousoulas K.G., Storz J.;
RT "Structures of and allelic diversity and relationships among the major
RT outer membrane protein (ompA) genes of the four chlamydial species.";
RL J. Bacteriol. 175:487-502(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-322, AND EPITOPE MAPPING.
RC STRAIN=MoPn / Nigg;
RX PubMed=1718870; DOI=10.1128/iai.59.11.4147-4153.1991;
RA Peterson E.M., Cheng X., Markoff B.A., Fielder T.J., de la Maza L.M.;
RT "Functional and structural mapping of Chlamydia trachomatis species-
RT specific major outer membrane protein epitopes by use of neutralizing
RT monoclonal antibodies.";
RL Infect. Immun. 59:4147-4153(1991).
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 -!- CAUTION: Was originally (PubMed:1937036 and PubMed:1718870) thought to
CC originate from Chlamydia trachomatis. {ECO:0000305}.
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DR EMBL; M64171; AAA23144.1; -; Genomic_DNA.
DR EMBL; U60196; AAB07068.1; -; Genomic_DNA.
DR EMBL; X63409; CAA45006.1; -; Genomic_DNA.
DR EMBL; AE002160; AAF38941.1; -; Genomic_DNA.
DR EMBL; M73044; AAD29101.1; -; Genomic_DNA.
DR PIR; C81747; C81747.
DR PIR; JT0947; JT0947.
DR PIR; S16034; S16034.
DR RefSeq; WP_010232357.1; NZ_CP027217.1.
DR AlphaFoldDB; P75024; -.
DR STRING; 243161.TC_0052; -.
DR EnsemblBacteria; AAF38941; AAF38941; TC_0052.
DR KEGG; cmu:TC_0052; -.
DR eggNOG; ENOG502ZVFZ; Bacteria.
DR HOGENOM; CLU_693881_0_0_0; -.
DR Proteomes; UP000000800; 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; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..387
FT /note="Major outer membrane porin"
FT /id="PRO_0000020139"
FT CONFLICT 118
FT /note="F -> Y (in Ref. 5; AAD29101)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Y -> F (in Ref. 5; AAD29101)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="L -> F (in Ref. 1; AAA23144)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="A -> P (in Ref. 1; AAA23144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42010 MW; 4FD6FDC23248E0A2 CRC64;
MKKLLKSVLA FAVLGSASSL HALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISL
RLGYYGDFVF DRVLKTDVNK QFEMGAAPTG DADLTTAPTP ASRENPAYGK HMQDAEMFTN
AAYMALNIWD RFDVFCTLGA TSGYLKGNSA AFNLVGLFGR DETAVAADDI PNVSLSQAVV
ELYTDTAFAW SVGARAALWE CGCATLGASF QYAQSKPKVE ELNVLCNAAE FTINKPKGYV
GQEFPLNIKA GTVSATDTKD ASIDYHEWQA SLALSYRLNM FTPYIGVKWS RASFDADTIR
IAQPKLETSI LKMTTWNPTI SGSGIDVDTK ITDTLQIVSL QLNKMKSRKS CGLAIGTTIV
DADKYAVTVE TRLIDERAAH VNAQFRF
