OMCA_CHLTR
ID OMCA_CHLTR Reviewed; 88 AA.
AC P0CC05; P21355; Q57433;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 43.
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=omp2A, omp3; OrderedLocusNames=CT_444;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B/Tw-5/OT;
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 [GENOMIC DNA].
RC STRAIN=C/TW-3, and F/IC-Cal-13;
RA Zhang Y.-X., Caldwell H.D.;
RT "The nucleotide sequences of 10 and 60 kDa cysteine-rich outer membrane
RT protein genes of Chlamydia trachomatis serovar F.";
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; X54451; CAA38318.1; -; Genomic_DNA.
DR EMBL; M85196; AAA23153.1; -; Genomic_DNA.
DR EMBL; M85197; AAA23158.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC68043.1; -; Genomic_DNA.
DR PIR; E71513; E71513.
DR PIR; S12126; S12126.
DR RefSeq; NP_219956.1; NC_000117.1.
DR RefSeq; WP_009871799.1; NC_000117.1.
DR AlphaFoldDB; P0CC05; -.
DR STRING; 813.O172_02420; -.
DR TCDB; 1.B.2.1.2; the chlamydial porin (cp) family.
DR EnsemblBacteria; AAC68043; AAC68043; CT_444.
DR GeneID; 884216; -.
DR KEGG; ctr:CT_444; -.
DR PATRIC; fig|272561.5.peg.479; -.
DR HOGENOM; CLU_2463467_0_0_0; -.
DR OMA; PDGRCKQ; -.
DR Proteomes; UP000000431; 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; Reference proteome; 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_0000018158"
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; CAA38318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 88 AA; 9206 MW; D9592F84EEC7DA1B CRC64;
MKKTALLAAL CSVVSLSSCC RIVDCCFEDP CAPIQCSPCE SKKKDVDGGC NSCNGYVPAC
KPCGGDTHQD AKHGPQARGI PVDGKCRQ
