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Database: UniProt
Entry: Q87XU6_PSESM
LinkDB: Q87XU6_PSESM
Original site: Q87XU6_PSESM 
ID   Q87XU6_PSESM            Unreviewed;      1161 AA.
AC   Q87XU6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=PSPTO_4079 {ECO:0000313|EMBL:AAO57536.1};
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO57536.1, ECO:0000313|Proteomes:UP000002515};
RN   [1] {ECO:0000313|EMBL:AAO57536.1, ECO:0000313|Proteomes:UP000002515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA   Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA   Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA   D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA   Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA   Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AE016853; AAO57536.1; -; Genomic_DNA.
DR   RefSeq; NP_793841.1; NC_004578.1.
DR   AlphaFoldDB; Q87XU6; -.
DR   STRING; 223283.PSPTO_4079; -.
DR   KEGG; pst:PSPTO_4079; -.
DR   PATRIC; fig|223283.9.peg.4181; -.
DR   eggNOG; COG1457; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_008084_1_0_6; -.
DR   OrthoDB; 9810730at2; -.
DR   PhylomeDB; Q87XU6; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.10.4160.10; Hydantoin permease; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AAO57536.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002515};
KW   Transferase {ECO:0000313|EMBL:AAO57536.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        83..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        466..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        609..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        651..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          726..941
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          964..1075
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1013
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1161 AA;  129344 MW;  D44DDB52A06A7E26 CRC64;
     MIAHLRKPRA WILLAFVVQR LFYQGASNDL LPLLWRRTVR PSGSQRIIKI RRDYNRLVAD
     ETMEDYALRF TPKSFRKWSE WRISNTAVGA VSFLALEAIG GALVISYGFT NTLWAILATA
     LVIFLTGLPI SYYAARYGVD MDLLTRGAGF GYIGSTITSL IYASFTFLFF ALEAAIMALA
     LELYFHIPIA LAYIICSIIV IPLAVYGVTL ISRLQMWSQP LWLTLLLVPY VFVIWKNPDA
     LGDWLSFSGR EGEGGTFDLL FFGAAFSVAL SLVTQIGEQV DYLRFLPEKT RHNRKRWWAA
     LLMAGPGWII PGALKIMAGA FLAFLALQHE VPVERAAEPT QMYLVAFRYV FSSPEWALAA
     MTLFVIISQI KINMTNAYAG SLAWSNFFVR VTHSHPGRVV WLVFNVAIAL VLMELGVFDA
     IEQVLGLYAN VAIAWIGALV ADLVINKPMG WSPKHIEFKR AHLYDINPVG VGAMSIASLV
     SFCAHFGLFG AIAQAAPPLI SLAIALVTAP LLAWLTDGKY YIARTSSDTL LYPQGRQESL
     LCGLCNNAFE TPDMAYCPAY RTPICSLCCS LDARCGDQCK PRARLSMQFE DLIGKVLPRF
     PRHYLHTRLA QYLGLLTILV AGSSGALALI YNQVAHGLID QSPEAHHLLM LAFLKAFLTV
     CVFAGVLAWW VVLTRESRRV AQEESERQTS LLIQEIDAHE KTDQALQKAK EASEAANAAK
     SRYITGLSHE LRTPLNSILG FTQILQRDTT TPPHHQDPLA TIMRSSSHLL SLINGLLDVA
     KIEAGKLKLE PTEILFQEFL HDLEKMFAGT AQEKNLGFRL ELEGRMPMVV RGDEKRVRQI
     LINLLGNAVN FTDSGEVVLR VSYRRETAIF DIVDSGIGIA PEQIERIFQP FERGGQTRHD
     NGVGLGLTIT RMLTALMGGA LSVSSTPGEG THFKVRLFLS EVRVPKAVID VNHDVVGYDG
     ERRLVLVVDD HIEHRKVISG MLEPLGFTVA QAENGMEAVR QVSLLHPDLI LMDLSMPDMD
     GWATLRMIRR NARSNAPVIV LSANANASTD DDIGHDYLSK PVHLRDLLDR LKHHLNLNWQ
     HRSRTASETK TPWILPPRED LEDLYTLCGL GYVRGIQNKL DAIETSNIAS GSFVTDLRAL
     AKGFRLDELS LHLKEMLDER P
//
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