ID W4SKT5_9XANT Unreviewed; 1092 AA.
AC W4SKT5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=XPR_3815 {ECO:0000313|EMBL:GAE57180.1};
OS Xanthomonas arboricola pv. pruni MAFF 301420.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1418095 {ECO:0000313|EMBL:GAE57180.1, ECO:0000313|Proteomes:UP000019084};
RN [1] {ECO:0000313|EMBL:GAE57180.1, ECO:0000313|Proteomes:UP000019084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 301420 {ECO:0000313|Proteomes:UP000019084};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAE57180.1}.
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DR EMBL; BAVC01000318; GAE57180.1; -; Genomic_DNA.
DR AlphaFoldDB; W4SKT5; -.
DR Proteomes; UP000019084; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..630
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 705..818
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 827..943
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 973..1089
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 310..386
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 754
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 876
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1022
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1092 AA; 118569 MW; D30762BE8A53800B CRC64;
MREGCVQADP AAERQNPGDL RVKLIGYHDR PPCPVRAFMQ NISTTRDRWV WVIAGALMAG
TLGVELVTPL GYAVWLTYFV AVGVTVFQNR VQVPLVVTAL SCVLLAVGFQ LAPSSTSSSF
SSINRSIGGV SFLAMALVVM QAIRARRQAE LALWLQQAEN TVEANLRGDH SPDDLANAAV
RALCDTLDAQ VGALYRIEGE RLRLTGAAAL PADASRTLPT DAGQLGEALR SGTVRRVRGV
EAGHLQIASG LGRSACQELL LAPLIADGRV IGILELGRAA AQGTARTREE ELLTRCGENI
GLALRTALLR AQLVALLEET QRQSEELQTQ QEELRVANEE LEEQSRSLQQ SQSDLELQQA
ELEQTNVQLE ERTQALEAQK QALLIAQNQL VRNSNELSTA SRYKSEFLAN MSHELRTPLN
SALILAKLLS DNKDGTLSPE QVKYAQAILS SNNDLLALIN DILDLSKIEA GHVELADETV
ATSSVLQRLR ETFEPLARQK GLALQLAAES DAPTQLVVDS QRLQQILKNL LANAIKFTEH
GSVSLSIQAH TPGRVLFKVN DTGIGIVHEQ TEVIFEAFRQ ADGSTRRRYG GTGLGLSISR
DLAQRMGGSI RVDSQPGRGS CFTLELPIDG APAELVTAAQ ANAGAMAIGT APSSQSASGT
AMASRLDGRA TVASTEMPLP IPAAAAPPLQ RADDDRDQRT RPGRLILAVE DEARFAQALV
DLAHELDFDC VVAPSAEEAL RLATELRPSG ILLDIGLPDA SGLSVLERLK RDPATRHIPV
HVVSALERSQ IALELGAVGY LIKPATRELL AGAIRQLEDT NARAVRRLLI VEDDSALRAN
LQLLLARDQL EIIAVGSIAE AMQQLAGSTF DCMVTDLALP DGSGYDLLER MAGNDAVAFP
PVIVYTGRAL TRDEEQRLRR YSKSIIIKGV RSPERLLDEV TLFLHSVEAS LPSDQQRLLR
EARRRDAVLD GATVLLAEDD VRNIFALSSV LEPLGVTLQI ARNGREALEH LAKHEVDLVL
MDIMMPEMDG LTAMRQIRAN RQWQDLPIIA LTAKAMADDR ERCLEAGAND YIAKPIDVDK
LVSLCRVWCS RQ
//
