OMCA_CHLT2
ID OMCA_CHLT2 Reviewed; 88 AA.
AC B0B816; P18585; P21356;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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; Synonyms=omp3; OrderedLocusNames=CTL0703;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=2287277; DOI=10.1111/j.1365-2958.1990.tb02065.x;
RA Allen J.E., Cerrone M.C., Beatty P.R., Stephens R.S.;
RT "Cysteine-rich outer membrane proteins of Chlamydia trachomatis display
RT compensatory sequence changes between biovariants.";
RL Mol. Microbiol. 4:1543-1550(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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.
CC -!- DEVELOPMENTAL STAGE: It is present but the disulfide bonds are reduced
CC in reticulate bodies (RBs).
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DR EMBL; X54450; CAA38316.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP04142.1; -; Genomic_DNA.
DR PIR; S12125; S12125.
DR RefSeq; WP_009873814.1; NC_010287.1.
DR RefSeq; YP_001654775.1; NC_010287.1.
DR AlphaFoldDB; B0B816; -.
DR EnsemblBacteria; CAP04142; CAP04142; CTL0703.
DR KEGG; ctb:CTL0703; -.
DR PATRIC; fig|471472.4.peg.755; -.
DR HOGENOM; CLU_2463467_0_0_0; -.
DR OMA; PDGRCKQ; -.
DR Proteomes; UP000000795; Chromosome.
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 2: Evidence at transcript level;
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_0000417576"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> R (in Ref. 1; CAA38316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 88 AA; 9279 MW; D35B0584EEC7DA1B CRC64;
MKKTALLAAL CSVVSLSSCC RIVDCCFEDP CAPIQCSPCE SKKKDVDGGC NSCNGYVPAC
KPCGGDTHQD AEHGPQAREI PVDGKCRQ