ID A0A1Y0KLJ1_9PSED Unreviewed; 1169 AA.
AC A0A1Y0KLJ1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B9K09_00310 {ECO:0000313|EMBL:ARU86531.1};
OS Pseudomonas sp. M30-35.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1981174 {ECO:0000313|EMBL:ARU86531.1, ECO:0000313|Proteomes:UP000196445};
RN [1] {ECO:0000313|EMBL:ARU86531.1, ECO:0000313|Proteomes:UP000196445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M30-35 {ECO:0000313|EMBL:ARU86531.1,
RC ECO:0000313|Proteomes:UP000196445};
RA He A., Zhao Q., Li H., Zhang J.;
RT "Complete genome sequence of the plant growth-promoting rhizobacterium
RT Pseudomonas rhizovicinus strain M30-35.";
RL Submitted (APR-2017) 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};
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DR EMBL; CP020892; ARU86531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0KLJ1; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000196445; Chromosome.
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; cd19410; HK9-like_sensor; 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; IPR007891; CHASE3.
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; PF05227; CHASE3; 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; 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, ECO:0000313|EMBL:ARU86531.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000196445};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..720
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 778..891
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 900..1016
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1046..1163
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 393..469
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 827
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 949
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1096
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1169 AA; 130693 MW; 497E823405AC6BBE CRC64;
MTKSAPNSEQ SFRQLVRRNI ALPLVIGLAT AVFFIGLIAY LINTQKTVDH TDQVISSASQ
SIKLTIDLET SLRGYLITGE NDFLQPYEEA RPLIKVELEN LEKMLKDDPD QSARLERIQA
LHEDWDRYAT GLIKLRQENA DIRNPVRSGR GKHITDSARE EYDNFIQIEQ QRRHQRNQQV
NDSVTLYVLL YILGSLTLSC LLAYFGRRDL LGLAAQHAQI LDQQRQSTEI IEHKAWLRSG
QSLLAEQVLG QANLQALGRN VLSCLTAYLN ASVGAFYVRS EQGDISRIAS YGFSRELENA
EQNFTSNETL VGQTASENKL LQLDNLPNAY LKVSSGLGST APVSIVLLPI SNGYSVNGVL
ELGFLQPIAP RVSEFLELIA EPVGTSIDSV RNRQRLQEIL SETQQLNEEL QVQQEELRTA
NEKLEEQSQV LKESQAYLET QQAELEQTNE QLADQAQILA EQRDTLDERN TALGRVQVLL
EERAQELQRA SLYKSEFLAN MSHELRTPLN SSLILAKLLA DNPQGNLTAE QTKFAESIYS
AGNDLLNLIN DILDISKVEA GKLEVRLHDV KLERLIEGMR NVFEPLANDK NLEFTIELLA
GVPDEIFSDQ QRIEQILKNL LSNAIKFTEK GCVTLTVSRQ PGAGIAFAVE DSGIGIREDQ
QESIFEAFRQ ADGAINRRYG GTGLGLSISR DLAALLGGSI SIVSTPGAGS TFTLLLPETY
DETAANALTD LNSGPAATPV QQPIKIAQAS VPVPVVTEPV MLPRFADDRE QLPEAGRCVL
VIEDEPKFAQ ILYDLAHELE YNCLVAHGAD EGVELASKLL PQGILLDMRL PDASGLTVLQ
RLKNNPLTRH IPVHVISVED RIEAALQLGA IGYAVKPTTR EHLKAVFAKL EAKLSQQVKR
VLLVEDDALQ RESISHLIGD DDIEITAVEF GQQALDLLRT TVFDCMIIDL KLPDMQGNQL
LKRMSAEDIR AFPPVIVYTG RNLTRDEETD LMKYSKSIII KGARSPERLL DEVTLFLHKV
ESQLSTERQT MLKTARNRDK VFEGRRILLV DDDVRNIFAL TNALEQKGAV VEVGCNGREA
IEKLNQFDDI DLVLMDIMMP EMDGYEATEI IRKDPRWRKL PIIAVTAKAM KDDQDRCLRA
GANDYLAKPI DLERLFSLIR VWMPKLERI
//
