OMPB_RICPR
ID OMPB_RICPR Reviewed; 1643 AA.
AC Q53020; Q9ZCM0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Outer membrane protein B;
DE AltName: Full=168 kDa surface-layer protein;
DE AltName: Full=Cell surface antigen 5;
DE Short=Sca5;
DE AltName: Full=Surface protein antigen;
DE AltName: Full=rOmp B;
DE Short=rOmpB;
DE Contains:
DE RecName: Full=120 kDa surface-exposed protein;
DE AltName: Full=120 kDa outer membrane protein OmpB;
DE AltName: Full=Surface protein antigen;
DE AltName: Full=p120;
DE Contains:
DE RecName: Full=32 kDa beta peptide;
DE Flags: Precursor;
GN Name=ompB; Synonyms=spa, spaP; OrderedLocusNames=RP704;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC VR-142 / Breinl;
RX PubMed=2122457; DOI=10.1073/pnas.87.21.8237;
RA Carl M., Dobson M.E., Ching W.M., Dasch G.A.;
RT "Characterization of the gene encoding the protective paracrystalline-
RT surface-layer protein of Rickettsia prowazekii: presence of a truncated
RT identical homolog in Rickettsia typhi.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8237-8241(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC VR-142 / Breinl;
RA Moron C.G., Yu X.J., Walker D.H.;
RT "Sequence analysis of ompB of Rickettsia prowazekii.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC VR-142 / Breinl;
RX PubMed=1370573; DOI=10.1016/0161-5890(92)90161-p;
RA Ching W.M., Carl M., Dasch G.A.;
RT "Mapping of monoclonal antibody binding sites on CNBr fragments of the S-
RT layer protein antigens of Rickettsia typhi and Rickettsia prowazekii.";
RL Mol. Immunol. 29:95-105(1992).
RN [5]
RP PROTEIN SEQUENCE OF 1353-1369, AND CLEAVAGE SITE.
RC STRAIN=ATCC VR-142 / Breinl;
RX PubMed=1729180; DOI=10.1128/iai.60.1.159-165.1992;
RA Hackstadt T., Messer R., Cieplak W. Jr., Peacock M.G.;
RT "Evidence for proteolytic cleavage of the 120-kilodalton outer membrane
RT protein of rickettsiae: identification of an avirulent mutant deficient in
RT processing.";
RL Infect. Immun. 60:159-165(1992).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ADHESION TO BIOTINYLATED
RP EUKARYOTIC CELLS.
RC STRAIN=ATCC VR-142 / Breinl;
RX PubMed=16574381; DOI=10.1016/j.resmic.2006.02.002;
RA Renesto P., Samson L., Ogata H., Azza S., Fourquet P., Gorvel J.-P.,
RA Heinzen R.A., Raoult D.;
RT "Identification of two putative rickettsial adhesins by proteomic
RT analysis.";
RL Res. Microbiol. 157:605-612(2006).
CC -!- FUNCTION: The 120 kDa surface-exposed protein is a major structural
CC protein which may play a role as a rickettsial virulence factor and/or
CC immunogen during infection.
CC -!- FUNCTION: The 32 kDa beta peptide may serve as a membrane anchor. It
CC has been shown to adhere to biotinylated Vero cell proteins.
CC -!- SUBCELLULAR LOCATION: [Outer membrane protein B]: Periplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [120 kDa surface-exposed protein]: Secreted. Cell
CC surface. Note=Surface exposed. This bacterium is covered by a S-layer
CC with hexagonal symmetry.
CC -!- SUBCELLULAR LOCATION: [32 kDa beta peptide]: Cell outer membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The
CC cleaved C-terminal fragment (autotransporter domain) is localized in
CC the outer membrane.
CC -!- SIMILARITY: Belongs to the rickettsiae OmpA/OmpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M37647; AAA26390.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF161079; AAD42234.1; -; Genomic_DNA.
DR EMBL; AJ235273; CAA15140.1; -; Genomic_DNA.
DR PIR; D71630; D71630.
DR RefSeq; NP_221064.1; NC_000963.1.
DR RefSeq; WP_010886353.1; NC_000963.1.
DR AlphaFoldDB; Q53020; -.
DR SMR; Q53020; -.
DR STRING; 272947.RP704; -.
DR EnsemblBacteria; CAA15140; CAA15140; CAA15140.
DR KEGG; rpr:RP704; -.
DR PATRIC; fig|272947.5.peg.725; -.
DR eggNOG; COG4625; Bacteria.
DR HOGENOM; CLU_000413_0_0_5; -.
DR OMA; DITQNSG; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR022095; rOmpB.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF12334; rOmpB; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Membrane; Periplasm;
KW Reference proteome; Secreted; Transmembrane; Transmembrane beta strand;
KW Virulence.
FT CHAIN 1..1643
FT /note="Outer membrane protein B"
FT /id="PRO_0000387581"
FT CHAIN 1..1328
FT /note="120 kDa surface-exposed protein"
FT /id="PRO_0000032654"
FT PROPEP 1329..1352
FT /evidence="ECO:0000255"
FT /id="PRO_0000032655"
FT CHAIN 1353..1643
FT /note="32 kDa beta peptide"
FT /id="PRO_0000032656"
FT DOMAIN 1355..1643
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT VARIANT 257
FT /note="V -> A (in strain: Breinl)"
FT VARIANT 1010
FT /note="Y -> D (in strain: Breinl)"
FT VARIANT 1450
FT /note="A -> S (in strain: Breinl)"
FT CONFLICT 178..179
FT /note="AA -> VC (in Ref. 1; AAA26390)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..201
FT /note="TTQEAPLTLGA -> INSRSSSYHLVS (in Ref. 1; AAA26390)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="T -> I (in Ref. 1; AAA26390)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="Q -> L (in Ref. 1; AAA26390)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="D -> G (in Ref. 2; AAD42234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="T -> S (in Ref. 2; AAD42234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1643 AA; 169855 MW; 735FDF392E6346CC CRC64;
MAQKPNFLKK IISAGLVTAS TATIVAGFSG VAMGAAMQYN RTTNAAATTF DGIGFDQAAG
ANIPVAPNSV ITANANNPIT FNTPNGHLNS LFLDTANDLA VTINEDTTLG FITNIAQQAK
FFNFTVAAGK ILNITGQGIT VQEASNTINA QNALTKVHGG AAINANDLSG LGSITFAAAP
SVLEFNLINP TTQEAPLTLG ANSKIVNGGN GTLNITNGFI QVSDNTFAGI KTINIDDCQG
LMFNSTPDAA NTLNLQVGGN TINFNGIDGT GKLVLVSKNG AATEFNVTGT LGGNLKGIIE
LNTAAVAGKL ISQGGAANAV IGTDNGAGRA AGFIVSVDNG NAATISGQVY AKNMVIQSAN
AGGQVTFEHI VDVGLGGTTN FKTADSKVII TENSNFGSTN FGNLDTQIVV PDTKILKGNF
IGDVKNNGNT AGVITFNANG ALVSASTDPN IAVTNINAIE AEGAGVVELS GIHIAELRLG
NGGSIFKLAD GTVINGPVNQ NALMNNNALA AGSIQLDGSA IITGDIGNGG VNAALQHITL
ANDASKILAL DGANIIGANV GGAIHFQANG GTIKLTNTQN NIVVNFDLDI TTDKTGVVDA
SSLTNNQTLT INGSIGTVVA NTKTLAQLNI GSSKTILNAG DVAINELVIE NNGSVQLNHN
TYLITKTINA ANQGQIIVAA DPLNTNTTLA DGTNLGSAEN PLSTIHFATK AANADSILNV
GKGVNLYANN ITTNDANVGS LHFRSGGTSI VSGTVGGQQG HKLNNLILDN GTTVKFLGDT
TFNGGTKIEG KSILQISNNY TTDHVESADN TGTLEFVNTD PITVTLNKQG AYFGVLKQVI
ISGPGNIVFN EIGNVGIVHG IAANSISFEN ASLGTSLFLP SGTPLDVLTI KSTVGNGTVD
NFNAPIVVVS GIDSMINNGQ IIGDKKNIIA LSLGSDNSIT VNANTLYSGI RTTKNNQGTV
TLSGGMPNNP GTIYGLGLEN GSPKLKQVTF TTDYNNLGSI IANNVTINDY VTLTTGGIAG
TDFDAKITLG SVNGNANVRF VDSTFSDPRS MIVATQANKG TVTYLGNALV SNIGSLDTPV
ASVRFTGNDS GAGLQGNIYS QNIDFGTYNL TILNSNVILG GGTTAINGEI DLLTNNLIFA
NGTSTWGDNT SISTTLNVSS GNIGQVVIAE DAQVNATTTG TTTIKIQDNA NANFSGTQAY
TLIQGGARFN GTLGAPNFAV TGSNIFVKYE LIRDSNQDYV LTRTNDVLNV VTTAVGNSAI
ANAPGVSQNI SRCLESTNTA AYNNMLLAKD PSDVATFVGA IATDTSAAVT TVNLNDTQKT
QDLLSNRLGT LRYLSNAETS DVAGSATGAV SSGDEAEVSY GVWAKPFYNI AEQDKKGGIA
GYKAKTTGVV VGLDTLASDN LMIGAAIGIT KTDIKHQDYK KGDKTDINGL SFSLYGSQQL
VKNFFAQGNA IFTLNKVKSK SQRYFFESNG KMSKQIAAGN YDNMTFGGNL IFGYDYNAMP
NVLVTPMAGL SYLKSSNENY KETGTTVANK RINSKFSDRV DLIVGAKVAG STVNITDIVI
YPEIHSFVVH KVNGKLSNSQ SMLDGQTAPF ISQPDRTAKT SYNIGLSANI KSDAKMEYGI
GYDFNSASKY TAHQGTLKVR VNF
