ID A0A0R0AQY1_9GAMM Unreviewed; 807 AA.
AC A0A0R0AQY1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ARC20_09970 {ECO:0000313|EMBL:KRG43364.1};
OS Stenotrophomonas panacihumi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG43364.1, ECO:0000313|Proteomes:UP000051802};
RN [1] {ECO:0000313|EMBL:KRG43364.1, ECO:0000313|Proteomes:UP000051802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG43364.1,
RC ECO:0000313|Proteomes:UP000051802};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (OCT-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 -!- 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:KRG43364.1}.
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; LLXU01000075; KRG43364.1; -; Genomic_DNA.
DR RefSeq; WP_057646448.1; NZ_PZOY01000006.1.
DR AlphaFoldDB; A0A0R0AQY1; -.
DR STRING; 676599.ARC20_09970; -.
DR OrthoDB; 9770473at2; -.
DR Proteomes; UP000051802; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051802}.
FT DOMAIN 11..127
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 145..215
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 217..269
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 364..415
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 428..655
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 678..793
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 123..155
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 729
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 807 AA; 88303 MW; DFF62E4D08AA80A8 CRC64;
MAEAQHPAPI RILMLEDSAL DAELIVAQLK RAHLAFTTER VWTRDDFLRA IQDGGHDVIL
ADHVLPGFDG DTALTLAREH APEIPFIFVS GTLTEELAVQ ALTRGARDYV VKQRLQRLPD
AVLRALAERE ERARLAHAEA ELQQSRDRLQ LITDSLPALI THFGTDHHFR FVNHASLDWY
GVPPEALVGQ SIQQAIGQDA FERARPHLER VLRGERVNFE THLPRADGSV RYAQVDGVPE
HDAHGAITGY YTLARDISDL KRAELSLRQI NESLEHQVLA RTADLRRSES RLQAVFQSSF
QHQNLLTIHG DIVQANVASL AAILSTLPEV AGQAFADSAW FAATPGAPEL IRAAVAAAAQ
GHESRHELEL QLPTGTRSFD FSFRPLQDPD GQVSAIVSEA VETTARRQAE AALRQSQKIE
AVGQLTGGIA HDFNNILTII AGNIEHARMM IDHLGDTAAR PARALDNAMR GVSRAASLTQ
RLLAFARQQP LQSQAVDIGA HMHGMQDMLQ RALGELVRLE VDVPTDAWCV ELDPAQLESA
ILNLAVNARD AMPEGGVLSI EAGNVHLDED YAAHHPDIAE GDYVRLRIRD TGHGMSHETM
TRVFEPFFTT KEVGRGTGLG LPMVYGFVKQ SGGHVLLEST PGVGTMVTLL FPRSDLPLPL
SREDAAPLMA GVDAPEETLL VAEDNDDVRA YTVEALRHLG YRVLEAHDGA SALRLLERPD
VRVDLLLSDI VMPGMSGWEL TQQAKLRKPD LRVLLTSGYP RDMAAHGSVA RGMSLLAKPF
TRADLSVAVR KALEMPVGET HVVGAAP
//
