ID   OMCA_CHLMU              Reviewed;          88 AA.
AC   Q9PJU9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Small cysteine-rich outer membrane protein OmcA;
DE            Short=Small-CRP;
DE   AltName: Full=9 kDa cysteine-rich lipoprotein;
DE            Short=9KD-CRP;
DE   Flags: Precursor;
GN   Name=omcA; OrderedLocusNames=TC_0728;
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 [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).
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; AE002160; AAF39538.1; -; Genomic_DNA.
DR   PIR; D81671; D81671.
DR   RefSeq; WP_010231362.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PJU9; -.
DR   EnsemblBacteria; AAF39538; AAF39538; TC_0728.
DR   GeneID; 1246091; -.
DR   KEGG; cmu:TC_0728; -.
DR   HOGENOM; CLU_2463467_0_0_0; -.
DR   OMA; PDGRCKQ; -.
DR   OrthoDB; 1958829at2; -.
DR   Proteomes; UP000000800; 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_0000018154"
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;  9342 MW;  00A00749DD1A364A CRC64;
     MKKTALLAAL CSVVSLSSCC RIVDCCFEDP CAPIKCSPCE SKKREVNGGC NSCNGYVPSC
     KPCGGELDHE TKQGPQARGI QADGRCRQ