ID A0A0D6SYR4_9PSED Unreviewed; 1373 AA.
AC A0A0D6SYR4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SZ55_1166 {ECO:0000313|EMBL:KIV73742.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV73742.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV73742.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV73742.1,
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:KIV73742.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYFT01000015; KIV73742.1; -; Genomic_DNA.
DR PATRIC; fig|1604022.3.peg.2856; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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; 3.30.450.350; CHASE domain; 1.
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; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Transferase {ECO:0000313|EMBL:KIV73742.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 70..259
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 336..407
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 410..462
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 477..526
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 570..622
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 640..861
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 878..1000
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1028..1146
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1190..1292
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 933
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1079
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1229
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1373 AA; 150105 MW; B9AE73FFA9AF5AC0 CRC64;
MIVVAWMLVV LGAGLLASLL VSQHQANRNQ SFIHQMLLND GKLIEHELIG RLDIYTYRLR
SIRGAIYMLQ LPNVTRDLLA RFGRVRDIEK EFPGARGFGF IRRVAPEDEA AFLRRTRADG
MPDFSIRQFA AHAGERYVIE FVDPAQRNQA AFGLDIASET RRRLAAVKAM NTGQPTLTAP
ITLVQESVEP SRAFLLLLPV YATPDTPPTV EERQRNTLGW AYAPLSMQEV MRSMTYPASD
LHLTLYDVVD SNTNHLIYDS LPDHVDDGVA SASFQREVYG RTWRFEISPH ANYIQRLELP
SPERVFGIGT LASLLLTGMT GALLVSRQRQ RTISAQQARL ATIIENSRDA IIGEALDGTI
VTWNPAAEQM FGYRADEVIG RPLAPLLVPP ERFSEDEDLL ERVSRGELGS TLETQRRHKQ
GHLIDVAITC SLIREPDGTI LAAAKLMHDI SDRLRAENYL REFSAKLELE VSQRTAELSR
LAGLLQGVLN ASSEVSIIAT DTHGRVAIFN RGAERLLGYR ADDAVGLLSI LSLHEQGEIN
RRGEELSAEA GRRVQGLEVL CLKADSQGAE TREWTYIRQD GSAVPVSMVM TAIRTTGGEA
IGYLSIAQDI TERRRSSEEL RAATVAAERA NAAKSLFLAN MSHEIRTPMN AVIGVAHLLQ
NTPLNEEQRN LLGKLEIAGR SLLGIINDIL DIAKIEAGEM RLESRPFSLR QLLQELGELF
SPQAEAKGLG FTLEGLDELP AQVLGDSLRI NQILMNLVGN ALKFTATGQI TVRVACREVD
AEQVRVTLTV VDTGCGIAAE VVDQLFSPFT QADASTTRRF GGTGLGLSVV RGLAEQMGGS
AGVRSVLGQG SEFWVEIPLE IAQTDLDATA TATARSLEVV VVDDSEADRQ QLARHCRGLG
WRVRMLDSGE ALLDLLRERV QHGLQLPDVL LVDWQMPGLD GVAVLEESAR ILAPTRLPSS
LLVSAHELDG YVRESGGLVD QALRKPVDSS SLFNAVNSAV VRHVGNTEKV MLGTDLDTRS
TRWLEGTRLL LVDDSEINLE VASLLLGQQG AEVDTAMNGR EAVQRLEQAP DHYDAVLMDV
QMPEMDGYEA TRTLRGKLGL TRLPVIALTA GALAEERRQA EAAGMNEFLS KPLEPTSLIR
TLRRLIEQFR LEPLPVRNLS ARLEQKDEQA WPVIPGIDAR EAANRLGNDI DLFLGSLNKL
FNEFADLEDT QLAQQLLSRD AATLAGKLHK LRGSAGLLGA MALHRACGDG ESSIRRPAGS
AEQRLALQQV SEALVALRAA AAPYLETQLS TPASGPQDAG EAEQALERLI TQLQGRDMAA
IDTFPDAVAA LLAKGGQALA DAAWKAVDDL QFDQALDVLA AHGLIDDEGS EHA
//
