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 27-MAR-2024, entry version 126. 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; Pseudomonadota; 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}. 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; 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 KEGG; rty:RT0699; -. DR eggNOG; COG4625; Bacteria. DR HOGENOM; CLU_000413_0_0_5; -. DR OrthoDB; 7161057at2; -. 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:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 1. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR036709; Autotransporte_beta_dom_sf. DR InterPro; IPR006315; OM_autotransptr_brl_dom. DR InterPro; IPR022095; OmpB_passenger_Rickettsia. DR InterPro; IPR048195; OmpB_ricketsia. DR NCBIfam; TIGR01414; autotrans_barl; 1. DR NCBIfam; NF041657; ompB_ricketsia; 1. DR Pfam; PF03797; Autotransporter; 1. DR Pfam; PF12334; rOmpB; 1. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; Autotransporter; 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 //