OMCA_CHLTJ
ID OMCA_CHLTJ Reviewed; 88 AA.
AC C4PRC2; P21355; Q57433;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Small cysteine-rich outer membrane protein OmcA;
DE Short=Small-CRP;
DE AltName: Full=9 kDa cysteine-rich lipoprotein;
DE Short=9kDa-CRP;
DE Flags: Precursor;
GN Name=omcA; OrderedLocusNames=JALI_4451;
OS Chlamydia trachomatis serovar B (strain Jali20/OT).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=580049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2612891; DOI=10.1016/0378-1097(89)90233-4;
RA Watson M.W., Lambden P.R., Ward M.E., Clarke I.N.;
RT "Chlamydia trachomatis 60 kDa cysteine rich outer membrane protein:
RT sequence homology between trachoma and LGV biovars.";
RL FEMS Microbiol. Lett. 53:293-297(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jali20/OT;
RX PubMed=19460133; DOI=10.1186/1471-2164-10-239;
RA Seth-Smith H.M.B., Harris S.R., Persson K., Marsh P., Barron A.,
RA Bignell A., Bjartling C., Clark L., Cutcliffe L.T., Lambden P.R.,
RA Lennard N., Lockey S.J., Quail M.A., Salim O., Skilton R.J., Wang Y.,
RA Holland M.J., Parkhill J., Thomson N.R., Clarke I.N.;
RT "Co-evolution of genomes and plasmids within Chlamydia trachomatis and the
RT emergence in Sweden of a new variant strain.";
RL BMC Genomics 10:239-239(2009).
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 large cysteine-rich periplasmic protein and the major outer membrane
CC porin. It has been described in publications as the Sarkosyl-insoluble
CC COMC (Chlamydia outer membrane complex), and serves as the functional
CC equivalent of peptidoglycan (By similarity). {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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=The protein moiety
CC probably penetrates into the periplasm.
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DR EMBL; X53510; CAA37587.1; -; Genomic_DNA.
DR EMBL; FM872308; CAX10899.1; -; Genomic_DNA.
DR RefSeq; WP_009871799.1; NC_012686.1.
DR AlphaFoldDB; C4PRC2; -.
DR KEGG; ctj:JALI_4451; -.
DR HOGENOM; CLU_2463467_0_0_0; -.
DR OMA; PDGRCKQ; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR003517; Cys-rich_OMP3_Chlamydia.
DR Pfam; PF03503; Chlam_OMP3; 1.
DR PRINTS; PR01335; CHLAMIDIAOM3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell shape; Disulfide bond; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..88
FT /note="Small cysteine-rich outer membrane protein OmcA"
FT /id="PRO_0000389551"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 88 AA; 9206 MW; D9592F84EEC7DA1B CRC64;
MKKTALLAAL CSVVSLSSCC RIVDCCFEDP CAPIQCSPCE SKKKDVDGGC NSCNGYVPAC
KPCGGDTHQD AKHGPQARGI PVDGKCRQ
