ID A0A1Y0KVT8_9PSED Unreviewed; 1177 AA.
AC A0A1Y0KVT8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B9K09_18695 {ECO:0000313|EMBL:ARU89874.1};
OS Pseudomonas sp. M30-35.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1981174 {ECO:0000313|EMBL:ARU89874.1, ECO:0000313|Proteomes:UP000196445};
RN [1] {ECO:0000313|EMBL:ARU89874.1, ECO:0000313|Proteomes:UP000196445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M30-35 {ECO:0000313|EMBL:ARU89874.1,
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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP020892; ARU89874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0KVT8; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000196445; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ARU89874.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000196445};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ARU89874.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1177
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011006307"
FT DOMAIN 308..362
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 381..433
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 451..672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 690..811
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 836..955
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1003..1097
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 744
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 888
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1042
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1177 AA; 130665 MW; 1B2354CE43334257 CRC64;
MARIGGLLLC WLLCFSVQAA QVPLSDEDQA WIKANPIIRV GVERDSWAPF DVIDEQGEYT
GLSGEYLQLL SKRLGMGVEV VLFDSWDAAV AALRADKVDL LPSVVRTPER EKFMRFTQPY
IVSSSLIFTR SGDRVQTLSD LDGHRVAVER GYVVEAGLKT KVPRIKLMQV ETTRDALQAL
SSGRVDAYVG DMIVASYLIR ELNLTNIEVR AEAGLTNSEF TFAVRMSAPE LQRAMDEALL
TVTDKETATI KAHWLPALTE FNWQRLIMVG WPYLLGIIAL ITFVLVWNRR LSVQIVERAR
AEAEAQLQRR TLTALINAIP DPIWFKDEKG NYAGINQACA ELFGLTREEV LGKNDMELLD
SEWAKARAGH DKVALSQHGA FETEGWALYP DGRRVVFDTV RTTFQDDQGA LLGLVGVSRD
ITVRKQAEEA LLAAKEMAED IARLRSDFLA NMSHEIRTPM NAIIGMSHLA LRADPSPRQR
DYLNKIQQSG QHLLGIINDI LDFSKVEAGE LKIEHIDFDL LQVLENVANL IGDKANEKNL
ELIFNLDPAV PQFLIGDPLR LGQVLINLAN NAVKFTDDGE IELLIRVDQR SIREVFIYFA
VRDTGIGISH EQISRLFQSF QQADTSTTRK YGGTGLGLAI CKKLIEAMGG EIGVESEQGK
GSLFWCSVPF GVSLEQDSLR DQPVVLKGRR VLVVDDNNTA RQVLHGLLGN LGMAVDVVES
GAQALSQIQH AIDQRSPYEL VMIDWQMPVM DGIETTRRLR ALELQNAPRV LMVTAYGREE
LLFSAKAAGI DGVLFKPVNP GLLREAVLRS LNAESPDSAI SSSRNQSSFP NFNGQRVLLV
EDNELNREVA AGLLEESGIL IEHAEHGGIA LDKLRANPDG YYSLVLMDMQ MPVLDGIGAT
QAIRKESRFA TLPVIAMTAN VLPTAREDCI RAGMNDHIGK PIDPHELWAT LKRWLDIKEP
RSQDTAAPIA TSKPKAIEAV PVAHNWYLPG VDVVTGLRRV LGKVELYQRL LTKFASSQHD
VPEQIRAAML AGEHEAAERL VHSLKGLAGN LGADDLLAKA GLLESAIQDP EHRQLDVHLQ
SVQNSVRELI AAILKQFPEA PPPDESPVDP ARIRELCMQL ERLLIEDDPR ASKFLEAQAV
ELRKFFKDDY DSLASAIRAY DFVRALRVVR DRSSGDT
//
