OMCBI_CHLTH
ID OMCBI_CHLTH Reviewed; 547 AA.
AC Q933I7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Large cysteine-rich periplasmic protein OmcB, serovars I/J;
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=ompA;
OS Chlamydia trachomatis.
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=I/UW-12, and J/UW-36;
RX PubMed=11567000; DOI=10.1128/jb.183.20.5997-6008.2001;
RA Millman K.L., Tavare S., Dean D.;
RT "Recombination in the ompA gene but not the omcB gene of Chlamydia
RT contributes to serovar-specific differences in tissue tropism, immune
RT surveillance, and persistence of the organism.";
RL J. Bacteriol. 183:5997-6008(2001).
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; AF304330; AAL14100.1; -; Genomic_DNA.
DR EMBL; AF304329; AAL14099.1; -; Genomic_DNA.
DR RefSeq; WP_009871798.1; NC_022121.1.
DR AlphaFoldDB; Q933I7; -.
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_0000248875"
FT CHAIN 41..547
FT /note="Large cysteine-rich periplasmic protein OmcB,
FT serovars I/J"
FT /id="PRO_0000248876"
FT REGION 45..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 58627 MW; 817BA3000FEA6A71 CRC64;
MNKLIRRAVT IFAVTSVASL FASGVLETSM AESLSTNVIS LADTKAKDNT SHKSKKARKN
HSKETPVDRK EVAPVHESKA TGPKQDSCFG RMYTVKVNDD RNVEITQAVP EYATVGSPYP
IEITATGKRD CVDVIITQQL PCEAEFVRSD PATTPTADGK LVWKIDRLGQ GEKSKITVWV
KPLKEGCCFT AATVCACPEI RSVTKCGQPA ICVKQEGPEN ACLRCPVVYK INVVNQGTAT
ARNVVVENPV PDGYAHSSGQ RVLTFTLGDM QPGEHRTITV EFCPLKRGCA TNIATVSYCG
GHKNTASVTT VINEPCVQVS IAGADWSYVC KPVEYVISVS NPGDLVLRDV VVEDTLSPGV
TVLEAAGAQI SCNKVVWTVK ELNPGESLQY KVLVRAQTPG QFTNNVVVKS CSDCGTCTSC
AEATTYWKGV AATHMCVVDT CDPVCVGENT VYRICVTNRG SAEDTNVSLM LKFSKELQPV
SFSGPTKGTI TGNTVVFDSL PRLGSKETVE FSVTLKAVSA GDARGEAILS SDTLTVPVSD
TENTHIY