(data stored in SCRATCH zone)

SWISSPROT: B4SSH9_STRM5

ID   B4SSH9_STRM5            Unreviewed;      1199 AA.
AC   B4SSH9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   SubName: Full=Multi-sensor hybrid histidine kinase {ECO:0000313|EMBL:ACF49861.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0156 {ECO:0000313|EMBL:ACF49861.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49861.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49861.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49861.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF49861.1; -; Genomic_DNA.
DR   RefSeq; WP_012509714.1; NC_011071.1.
DR   STRING; 391008.Smal_0156; -.
DR   EnsemblBacteria; ACF49861; ACF49861; Smal_0156.
DR   KEGG; smt:Smal_0156; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000056681; -.
DR   KO; K07679; -.
DR   OMA; MIHESAG; -.
DR   OrthoDB; 1755994at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00785-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.20.120.160; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00497; SBP_bac_3; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00062; PBPb; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; B4SSH9.
DR   SWISS-2DPAGE; B4SSH9.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Kinase {ECO:0000313|EMBL:ACF49861.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Transferase {ECO:0000313|EMBL:ACF49861.1}.
FT   DOMAIN      700    923       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      950   1069       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN     1104   1199       HPt. {ECO:0000259|PROSITE:PS50894}.
FT   COILED      595    615       {ECO:0000256|SAM:Coils}.
FT   COILED      670    690       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     999    999       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   MOD_RES    1143   1143       Phosphohistidine. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00110}.
SQ   SEQUENCE   1199 AA;  130838 MW;  B079687530460DA6 CRC64;
     MRSWAVRGLV LLLAVLVLPA APVQAVPGLL PLTPLQREYL AAHPSIVVGQ YDSGWPPFES
     LRDGQQVGLG PDYLSLLARQ LGVKVEARRY PDWTSVLDAA CRGEIDVVMN VGLSADRTRC
     MVYTAAYGEA PLALVGRPDD LRASDIPDLD GLRVVIEQDF LTGPQVRARF PRARQLVANS
     SLTALQMVRD DKADVYIGNA YVATELIASQ RLQGVVLLRP SDLPPEQLHF GIPNSKQPLA
     EALDLALAAT SQAQCDALVQ RWLPLPQWSA SARLALSQAE KRVLEQPLKI GFAPNAAPLS
     FADKEGKPSG LASEYLRRLL QAGANLQPEN SHDWYEVREK ARRGELQAVM GIPADSRYLG
     PDWVFSQPFI SVPNVIVSRV DSPALLGLSD LQGKRVLLSD PERIRGYVLQ QAPSARIIAA
     RSAEQALQRL AAGEADAYVG NLALVDHLLR SSFPGRLQVA APAGFNDQLV LAVERRHAAL
     ATTFDRLLLQ MTPRKREALR GDWLAVEYRN GIDWRHALRW GLPLLLVLLT ALLVHGIGYW
     RLRREVAGRR HLEQRLAEVT DNLPAVVYQA RRDADGTLGF PFIAGDLQAL FGITRQQAEQ
     DAKLLLERIE EEDRERILQA VEQAARQFAP LILEFRLRAD AGGARWVRSQ AHPYAAEAGA
     VTWSGYWVDV SEARAQAEAL TAAKAEAEQA AEAKSRFLAT MSHEIRTPMS GVLGMLEVLA
     HSPLDAEQQR ILGVIEDSAQ MLRQILDDIL DYSRLEAGAL RLEPVPQPLR PLLESVCRLL
     SAQASARGLA LLVEIDPQLA PAHEVDGVRL RQIVFNLLSN AIKFTARGEV RLQLEVLGPT
     AEDGSQPLCL SVTDTGMGIA PEQLQHLFAP FTQAGAYIQR DHGGTGLGLS ISQRLVQMMD
     GELTLHSTLG EGTRAEVRLS LVEAGSGDVE ALVAEQEQAS LLPPALRQAR VLVIEDHPTN
     QAMMAWRLQQ LGVPHVMVGD GQQGLDRLLS ESFDLVITDC RMPVLDGFGF TRLLREREGR
     NGQPRLTVLA LTASVLDDDA RRCREAGMDE VLAKPLSLAT LRAALLRWLP QAQGQSFAEP
     VTEVVADDGM ALPDLSTLQQ RFGSRAVAIQ LRDSLLQASE GDLAAVQRAL QAGDREAAAL
     HLHRQAGGLG AIGATVLAGQ ANALVERLQD AAETDPAPVF ASVAEFVARL QQQLQRLAH
//

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