OMPB_RICTY
ID OMPB_RICTY Reviewed; 1645 AA.
AC P96989;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=slp; OrderedLocusNames=RT0699;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=8224886; DOI=10.1016/0378-1119(93)90237-w;
RA Hahn M.-J., Kim K.-K., Kim I., Chang W.-H.;
RT "Cloning and sequence analysis of the gene encoding the crystalline surface
RT layer protein of Rickettsia typhi.";
RL Gene 133:129-133(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC VR-144 / Wilmington;
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 [4]
RP PROTEIN SEQUENCE OF 1353-1371, AND IDENTIFICATION OF CLEAVAGE SITE.
RC STRAIN=ATCC VR-144 / Wilmington;
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).
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.
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}.
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DR EMBL; L04661; AAB48987.1; -; Unassigned_DNA.
DR EMBL; AE017197; AAU04158.1; -; Genomic_DNA.
DR PIR; JN0896; JN0896.
DR RefSeq; WP_011191135.1; NC_006142.1.
DR AlphaFoldDB; P96989; -.
DR SMR; P96989; -.
DR STRING; 257363.RT0699; -.
DR EnsemblBacteria; AAU04158; AAU04158; RT0699.
DR KEGG; rty:RT0699; -.
DR eggNOG; COG4625; Bacteria.
DR HOGENOM; CLU_000413_0_0_5; -.
DR OMA; YPEVHAF; -.
DR OrthoDB; 7590at2; -.
DR Proteomes; UP000000604; 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 Secreted; Transmembrane; Transmembrane beta strand; Virulence.
FT CHAIN 1..1645
FT /note="Outer membrane protein B"
FT /id="PRO_0000387583"
FT CHAIN 1..1328
FT /note="120 kDa surface-exposed protein"
FT /id="PRO_0000032660"
FT PROPEP 1329..1352
FT /evidence="ECO:0000255"
FT /id="PRO_0000032661"
FT CHAIN 1353..1645
FT /note="32 kDa beta peptide"
FT /id="PRO_0000032662"
FT DOMAIN 1357..1645
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT CONFLICT 657
FT /note="H -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="V -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="G -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1306
FT /note="G -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1645 AA; 169698 MW; 0CB5641C7EB185EE CRC64;
MAQKPNFLKK IISAGLVTAS TATIVAGFSG VAMGAVMQYN RTTNAAATTV DGAGFDQTGA
GVNLPVATNS VITANSNNAI TFNTPNGNLN SLFLDTANTL AVTINENTTL GFVTNVTKQG
NFFNFTIGAG KSLTITGHGI TAQQAATTKS AQNVVSKVNA GAAINDNDLS GVGSIDFTAA
PSVLEFNLIN PTTQEAPLTL GDNAKIVNGA NGILNITNGF VKVSDKTFAG IKTINIGDNQ
GLMFNTTPDA ANALNLQGGG NTINFNGRDG TGKLVLVSKN GNATEFNVTG SLGGNLKGVI
EFDTTAAAGK LIANGGAANA VIGTDNGAGR AAGFIVSVDN GNAATISGQV YAKDIVIQSA
NAGGQVTFEH LVDVGLGGKT NFKTADSKVI ITENASFGST DFGNLAVQIV VPNNKILTGN
FIGDAKNNGN TAGVITFNAN GTLVSGNTDP NIVVTNIKAI EVEGAGIVQL SGIHGAELRL
GNAGSIFKLA DGTVINGPVN QNPLVNNNAL AAGSIQLDGS AIITGDIGNG AVNAALQDIT
LANDASKILT LSGANIIGAN AGGAIHFQAN GGTIQLTSTQ NNILVDFDLD VTTDQTGVVD
ASSLTNNQTL TINGSIGTIG ANTKTLGRFN VGSSKTILNA GDVAINELVM ENDGSVHLTH
NTYLITKTIN AANQGKIIVA ADPINTDTAL ADGTNLGSAE SPLSNIHFAT KAANGDSILH
IGKGVNLYAN NITTTDANVG SLHFRSGGTS IVSGTVGGQQ GLKLNNLILD NGTTVKFLGD
ITFNGGTKIE GKSILQISSN YITDHIESAD NTGTLEFVNT DPITVTLNKQ GAYFGVLKQV
MVSGPGNIAF NEIGNGVAHA IAVDSISFEN ASLGASLFLL SGTPLDVLTI KSTVGNGTVD
NFNAPILVVS GIDSMINNGQ VIGDQKNIIA LSLGSDNSIT VNSNTLYAGI RTTKTNQGTV
TLSGGIPNNP GTIYGLGLEN GDPKLKQVTF TTDYNNLGSI IATNVTINDD VTLTTGGIAG
TDFDGKITLG SINGNANVKF VDRTFSHPTS MIVSTKANQG TVTYLGNALV GNIGSSDIPV
ASVRFTGNDS GVGLQGNIHS QNIDFGTYNL TILNSDVILG GGTTAINGEI DLLTNNLIFA
NGTSTWGNNT SLSTTLNVSN GNVGQIVIAE GAQVNATTTG TTTIKIQDNA NANFSGTQTY
TLIQGGARFN GTLGAPNFDV TGNNIFVKYE LIRDANQDYV LTRTNDVLNV VTTAVGNSAI
ANAPGVHQNI AICLESTDTA AYNNMLLAKD SSDVATFIGA IATDTGAAVA TVNLNDTQKT
QDLLGNRLGA LRYLSNSETA DVGGSETGAV SSGDEAIDQV SYGVWAKPFY NIAEQDKKGG
LAGYKAKTAG VVVGLDTLAN DNLMIGAAIG ITKTDIKHQD YKKGDKTDIK GLSFSLYGAQ
QLVKNFFAQG SAIFTLNKVK SKSQRYFFDA NGKMNKQIAA GNYDNITFGG NLMFGYDYNA
LQGVLVTPMA GLSYLKSSNE NYKETGTTVA NKRIHSKFSD RIDLIVGAKV TGSAMNINDI
VIYPEIHSFV VHKVNGKLSK AQSMLDGQTA PFISQPDRTA KTSYNIGLSA NIRSDAKMEY
GIGYDFNAAS KYTAHQGTLK VRINF
