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OMCB_CHLT2
ID   OMCB_CHLT2              Reviewed;         547 AA.
AC   B0B815; P18586; P21354;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   25-MAY-2022, entry version 62.
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   Contains:
DE     RecName: Full=Large cysteine-rich periplasmic protein OmcB, isoform 1;
DE   Contains:
DE     RecName: Full=Large cysteine-rich periplasmic protein OmcB, isoform 2;
DE   Flags: Precursor;
GN   Name=omcB; Synonyms=omp2, omp2B; OrderedLocusNames=CTL0702;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-32 AND 41-51,
RP   DEVELOPMENTAL STAGE, AND EXISTENCE OF TWO MATURE FORMS.
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=2914847; DOI=10.1128/jb.171.1.285-291.1989;
RA   Allen J.E., Stephens R.S.;
RT   "Identification by sequence analysis of two-site posttranslational
RT   processing of the cysteine-rich outer membrane protein 2 of Chlamydia
RT   trachomatis serovar L2.";
RL   J. Bacteriol. 171:285-291(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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 protein. It
CC       has been described in publications as the Sarkosyl-insoluble COMC
CC       (Chlamydia outer membrane complex), and serves as the functional
CC       equivalent of peptidoglycan.
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).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: It is present but the disulfide bonds are reduced
CC       in the intracellular reticulate bodies (RBs).
CC       {ECO:0000269|PubMed:2914847}.
CC   -!- MISCELLANEOUS: In strain L2 the origin of the observed doublet has been
CC       shown to be different post-translational cleavage.
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=CAP04141.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M23001; AAA23152.1; -; Genomic_DNA.
DR   EMBL; AM884176; CAP04141.1; ALT_INIT; Genomic_DNA.
DR   PIR; A32244; A32244.
DR   RefSeq; WP_013984953.1; NC_010287.1.
DR   RefSeq; YP_001654774.1; NC_010287.1.
DR   AlphaFoldDB; B0B815; -.
DR   SMR; B0B815; -.
DR   TCDB; 1.B.2.1.2; the chlamydial porin (cp) family.
DR   EnsemblBacteria; CAP04141; CAP04141; CTL0702.
DR   KEGG; ctb:CTL0702; -.
DR   PATRIC; fig|471472.4.peg.754; -.
DR   HOGENOM; CLU_029611_0_0_0; -.
DR   Proteomes; UP000000795; 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   1: Evidence at protein level;
KW   Cell shape; Direct protein sequencing; Disulfide bond; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:2914847"
FT   CHAIN           23..547
FT                   /note="Large cysteine-rich periplasmic protein OmcB,
FT                   isoform 1"
FT                   /id="PRO_0000417577"
FT   CHAIN           41..547
FT                   /note="Large cysteine-rich periplasmic protein OmcB,
FT                   isoform 2"
FT                   /id="PRO_0000417578"
FT   REGION          45..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  58782 MW;  78CEB41CCF98472D CRC64;
     MNKLIRRAVT IFAVTSVASL FASGVLETSM AEFISTNVIS LADTKAKDNT SHKSKKARKN
     HSKETPVNRK KVAPVHESKA TGPKQDSCFG RMYTVKVNDD RNVEITQAVP KYATVGSPYP
     VEITATGKRD CVDVIITQQL PCEAEFVRSD PATTPTADGK LVWKIDRLGQ GEKSKITVWV
     KPLKEGCCFT AATVCACPEI RSVTKCGQPA ICVKQEGPEN ACLRCPVVYK INVVNQGTAT
     ARNVVVENPV PDSYAHSSGQ RVLTFTLGDM QPGEHRTITV EFCPLKRGRA TNIAMVSYCG
     GHKNTASVTT VINEPCVQVS IAGADWSYVC KPVEYVISVS NPGDLVLRDV VVKDTLSPGV
     TVLEAAGAQI SCNKVVWTVK ELNPGESLQY KVLVRAQTPG QFTNNVVVKS CSDCGTCTSC
     AEATTYWKGV AATHMCVVDT CDPVCVGENT VYRICVTNRG SAEDTNVSLM LKFSKELQPV
     SFSGPTKGTI TGNTVVFDSL PRLGSKETVE FSVTLKAVSA GDARGEAILS SDTLTVPVSD
     TENTHIY
 
 
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