OMCB_CHLFF
ID OMCB_CHLFF Reviewed; 558 AA.
AC Q253E5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
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; Synonyms=omp15; OrderedLocusNames=CF0821;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
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}.
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DR EMBL; AP006861; BAE81593.1; -; Genomic_DNA.
DR RefSeq; WP_011458368.1; NC_007899.1.
DR AlphaFoldDB; Q253E5; -.
DR STRING; 264202.CF0821; -.
DR KEGG; cfe:CF0821; -.
DR eggNOG; COG1361; Bacteria.
DR HOGENOM; CLU_029611_0_0_0; -.
DR OMA; CEAEFVS; -.
DR OrthoDB; 1049286at2; -.
DR Proteomes; UP000001260; 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 InterPro; IPR003506; Chlam_OMP6.
DR InterPro; IPR001434; DUF11.
DR Pfam; PF03504; Chlam_OMP6; 1.
DR Pfam; PF01345; DUF11; 2.
DR PRINTS; PR01336; CHLAMIDIAOM6.
DR TIGRFAMs; TIGR01451; B_ant_repeat; 1.
PE 3: Inferred from homology;
KW Cell shape; Disulfide bond; Periplasm; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..40
FT /evidence="ECO:0000255"
FT /id="PRO_0000248866"
FT CHAIN 41..558
FT /note="Large cysteine-rich periplasmic protein OmcB"
FT /id="PRO_0000248867"
SQ SEQUENCE 558 AA; 59899 MW; 3842D1FF3B4388ED CRC64;
MSKLIRRVVT VLALTSMASS FASGKTEVAA AESLVTRFIA SAEASDSNIL QTTAKKIRFG
RNKNQKPEQK NNNAFCDKEF YPCEGGQCQS SVDTRQESCY GKMYSVRVND DCNVEISQAV
PEYATVGSPY PIEILAVGKK DCVNVVITQQ LPCEVEFVSS DPVTTPTSDS KLIWTIDRLG
QGERCKITVW VKPLKEGCCF TAATVCACPE LRSYTKCGQP AICIKQEGPE CACLRCPVCY
KIEVCNTGSA IARSVVVDNP VPDGYTHASG QRVLSFNLGD MRPGDSKCFT VEFCPQKRGK
VTNVATVSYC GGHKCSANVT TVINEPCVQV NISGADWSYV CKPVEYTIVV SNPGDLKLYD
VVIEDTAPSG ASILEAAGAE ICCNKAVWCI KEMCPGETLQ FKVVAKAQTP GKFTNQVVVK
TNSDCGTCTS CAEVTTHWKG LAATHMCVID TNDPICVGEN TVYRICVTNR GSAEDTNVSL
ILKFSKELQP VSSSGPTKGT ITGNTVVFDA LPKLGSKESV EFSVTLKGVA PGDARGEAIL
SSDTLTVPVA DTENTHVY