ID A0A0R0DDD5_9GAMM Unreviewed; 1138 AA.
AC A0A0R0DDD5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ABB28_05130 {ECO:0000313|EMBL:KRG75299.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG75299.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG75299.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG75299.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG75299.1}.
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DR EMBL; LDJK01000014; KRG75299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0DDD5; -.
DR PATRIC; fig|517011.3.peg.491; -.
DR Proteomes; UP000051386; Unassembled WGS sequence.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRG75299.1};
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:UP000051386};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 481..701
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 747..860
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 869..985
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1015..1136
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 409..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 796
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 918
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1069
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1138 AA; 122000 MW; 6769AA9070F987EC CRC64;
MTSTSHSRAA TQAGTAFRTL GPLLAVMLFF LGSGFLAGKN IHTIREGSAL VLRSQETMTA
LADVLSAVQD AETGQRGYLL TGDDNYLEPY RAALGVASTR LDTVKEALAD DPAQRDRLKL
LARRVQDKLD ELHETIEVRR TQGLEPTLAV VASNRGKAAM DDIRARLATM GAIELDKRAG
RLEEMESAYS AALSSGAASA ALGIVLTIFI AILLRRHTRA RERDAWLQRG RLELATATGG
DLDSGALARA SLGFLTRFTG AQAGMLFEPA ASGFRQVGAV GAAAEADGTH TLRASGSLLG
RAVDEKRVLV VSNVPPGYFT VASGLGQALP RHLVIAPSIH EGEVSGIIEL GFFGAVPAEV
VELLELASAD MAVALRSAAY RARLSELLAK TQRQTEALQV QSEELKVSNE ELEEQSRALR
GSQHELEEQQ AELEQTNSQL FDQSQQLEEE RDKLARANAA ILAEAHKVQR ASQYKSEFLA
NMSHELRTPL NSALILSKLL GDNRDGNLSA EQVKFARTIH SSGTDLLNLI NEILDLSKIE
AGHIEVHAER FGVEKLLSGI AALLGPVASE KGLSLDVLMM ADCPPVIESD RQRIEQILKN
LLSNALKFTE QGGVTVSASA GGEGEVVFTV TDTGIGIAPE QQVRIFEAFQ QADGSISRRY
GGTGLGLSIS QELARLLGGD ITVDSEPGKG SRFRLVVATR LANPGRPAVS VAMAPLEPAA
TGFAAPTAIA VQDVRPAAST GGNGRGLILI VEDDAAFGQI IGDLASEMGF RYRIAQSAGE
ALAAARAELP HAIVLDVGLP DQSGLSVLDV LKRDMHTRHI PIHVVSAMDH SRKALALGAV
GFLGKPATRE ALAEVLLSLE RRLSLRPRLV LVVEDDAVQL DAVRELLALA DVETIGARSA
AECLQALAEH SFDCMVLDLT LSDASGFELL EMLSAQSVDA LPPIIVYTGR VLSAAEEVRL
RRYSSSIIIK GARSPERLLD EVTLFLHKVV SELPESKQGM IRTAQHRDTA LEGRRVLVVE
DDVRNIYALM NVLEPHGCKV TIARNGQDAI DALTAAVSGP APIELVLMDI MMPVKDGLTA
TREIRQDRRF DTLPIIALTA KAMPDDQQQC IQAGANDYVA KPLDVDKLVS LIRVWLTA
//
