ID A0A0D6S8R8_9PSED Unreviewed; 1163 AA.
AC A0A0D6S8R8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SZ55_4229 {ECO:0000313|EMBL:KIV64973.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV64973.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV64973.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV64973.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-2015) 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}.
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:KIV64973.1}.
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DR EMBL; JYFT01000064; KIV64973.1; -; Genomic_DNA.
DR RefSeq; WP_044411098.1; NZ_JYFT01000064.1.
DR AlphaFoldDB; A0A0D6S8R8; -.
DR PATRIC; fig|1604022.3.peg.808; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
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; cd00130; PAS; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR013656; PAS_4.
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; PF08448; PAS_4; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KIV64973.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KIV64973.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1163
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002312405"
FT DOMAIN 311..365
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 384..436
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 454..674
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 692..809
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 831..950
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 984..1078
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 427..454
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 746
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 883
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1023
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1163 AA; 128184 MW; 7929D3DACB312511 CRC64;
MLRLLGRLVL LLLLGSSTCQ AAEPLEFSTA EARWLQEHGR IRVGLERKGW PPFDLMGEDG
SYQGISADFL RLLGERLGLG VEPVYFDDWP QAREALRRGE VDVVPSAAKT PERERWMAFS
DPYLTTTSLI YSRRETPYRS LEELAGRRVA VERGYAMEDR LRQRSRDLQL VETSDTEAAL
RALSSGRADA YVGNMMAAGY LIHRLNLSNL EVSGDPGLAG SALHFAVLRE QAMLAELLDH
ALASVTNSER EAILARWLPP ADSVDWHELL ALGWPYGLAV LVLVTFVLVW NRRLAVQVVE
RQRAEAEAQR QRSTLQALVD AIPDPIWFKD TGGRYLGANQ AFAELIGQDL DGLVGHTDAE
LLPTERARLR LIQDQAALAM SRPMESEDWV LQRDGRKLLY ATVRATFDDE DGHLLGLVGV
SRDVTARKQS EEALERAKEL AEEAARLKAD FLANMSHEIR TPMNAIVGMT HLALRAGPEP
RQRDYLEKIR QASQHLMGLI NDILDFSRIE AGKLEVEQID FDLTLVLENL AALVGERAAD
KGLELIFRID PQVPRHLVGD PLRIGQILIN FANNAVKFTE RGEVEVAVRG EPRAGGWLLQ
LSVRDTGIGL DAAQQARLFE SFQQADTSTT RRYGGSGLGL AICRRLAEAM GGDVGVDSQP
GEGSLFWCRL LLPIAPEQPQ PDLLRPDLLG LRALVVDDNP SARRAASDLL ASLALRAEHC
GDGEAALARL QEADAQGNPF SLVILDRHMP GLDGLETARR LAALPLGKTP WVLLASTTGE
GEPSVDVIDQ YLEKPLTLPR LLHAIHACQL QRQAAAPRSE ATHMPQFDGQ RVLLVEDHPL
NREVAGELLE MANLQVDLAE NGLDALDRLR WQPDGHYALV LMDMQMPVLD GLEATRRLRQ
EGRFARLPII AMTANALADD RERCLAAGMN DHIAKPIEPR ELWGTLSRWL GPRPAAAPPV
APPLPAWHLP GVDIADGIRR ALGREDAYRR LLVRFAEGQR DWSQRLRAAL ASGQRSQAER
QAHDLRGLSG SLGAHGLKAQ AATLEQALAD AAEPERIELL LTELEPPLLA LVGAIEAQQR
EAAAPPPAAA DDSAALARTC RQLARLLEED DPRAARLLDE QAGMLRSAFN EGYGALESAV
RAYDFETAHQ ALRALADQRE ITL
//
