ID   OMCB_CHLMU              Reviewed;         548 AA.
AC   Q9PJV0;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Large cysteine-rich periplasmic protein OmcB;
DE            Short=Large-CRP;
DE   AltName: Full=60 kDa CRP;
DE   AltName: Full=60 kDa outer membrane protein;
DE   AltName: Full=Cysteine-rich outer membrane protein;
DE   Flags: Precursor;
GN   Name=omcB; OrderedLocusNames=TC_0727;
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       small cysteine-rich protein and the major outer membrane porin. It has
CC       been described in publications as the Sarkosyl-insoluble COMC
CC       (Chlamydia outer membrane complex), and serves as the functional
CC       equivalent of peptidoglycan. It is present but the disulfide bonds are
CC       reduced in reticulate bodies (RBs) (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: Periplasm {ECO:0000305}.
CC   -!- CAUTION: Was thought to be an outer membrane protein as it is part of a
CC       disulfide cross-linked complex that is insoluble in the detergent
CC       Sarkosyl; however based on experiments in C.psittaci it is likely to be
CC       periplasmic. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39537.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39537.1; ALT_INIT; Genomic_DNA.
DR   PIR; C81671; C81671.
DR   RefSeq; WP_029589527.1; NZ_ACOV01000003.1.
DR   AlphaFoldDB; Q9PJV0; -.
DR   STRING; 243161.TC_0727; -.
DR   EnsemblBacteria; AAF39537; AAF39537; TC_0727.
DR   GeneID; 1246090; -.
DR   KEGG; cmu:TC_0727; -.
DR   eggNOG; COG1361; Bacteria.
DR   HOGENOM; CLU_029611_0_0_0; -.
DR   OrthoDB; 1049286at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; 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   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003506; Chlam_OMP6.
DR   InterPro; IPR001434; DUF11.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF03504; Chlam_OMP6; 1.
DR   Pfam; PF01345; DUF11; 3.
DR   PRINTS; PR01336; CHLAMIDIAOM6.
DR   TIGRFAMs; TIGR01451; B_ant_repeat; 2.
PE   3: Inferred from homology;
KW   Cell shape; Disulfide bond; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..40
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000248868"
FT   CHAIN           41..548
FT                   /note="Large cysteine-rich periplasmic protein OmcB"
FT                   /id="PRO_0000248869"
FT   REGION          45..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  59114 MW;  1203623161FE26EB CRC64;
     MNKLIRRAVT IFAVTSVASL FASGVLETSM AESLSTNVIS LADTKAKETT SHQKDRKARK
     NHQNRTSVVR KEVTAVRDTK AVEPRQDSCF GKMYTVKVND DRNVEIVQSV PEYATVGSPY
     PIEITAIGKR DCVDVIITQQ LPCEAEFVSS DPATTPTADG KLVWKIDRLG QGEKSKITVW
     VKPLKEGCCF TAATVCACPE IRSVTKCGQP AICVKQEGPE SACLRCPVTY RINVVNQGTA
     TARNVVVENP VPDGYAHASG QRVLTYTLGD MQPGEQRTIT VEFCPLKRGR VTNIATVSYC
     GGHKNTASVT TVINEPCVQV NIEGADWSYV CKPVEYVISV SNPGDLVLRD VVIEDTLSPG
     ITVVEAAGAQ ISCNKLVWTL KELNPGESLQ YKVLVRAQTP GQFTNNVVVK SCSDCGICTS
     CAEATTYWKG VAATHMCVVD TCDPICVGEN TVYRICVTNR GSAEDTNVSL ILKFSKELQP
     ISFSGPTKGT ITGNTVVFDS LPRLGSKETV EFSVTLKAVS AGDARGEAIL SSDTLTVPVS
     DTENTHIY