ID A0A1D8Y7Y1_9GAMM Unreviewed; 537 AA.
AC A0A1D8Y7Y1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BIZ42_05435 {ECO:0000313|EMBL:AOX61687.1};
OS Stenotrophomonas sp. LM091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX61687.1, ECO:0000313|Proteomes:UP000177427};
RN [1] {ECO:0000313|EMBL:AOX61687.1, ECO:0000313|Proteomes:UP000177427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM091 {ECO:0000313|EMBL:AOX61687.1,
RC ECO:0000313|Proteomes:UP000177427};
RA Lefeuvre P.;
RT "Complete genome sequence of a copper-resistant commensal bacteria:
RT Stenotrophomonas sp. strain LM091.";
RL Submitted (SEP-2016) 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};
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DR EMBL; CP017483; AOX61687.1; -; Genomic_DNA.
DR RefSeq; WP_070425791.1; NZ_CP017483.1.
DR AlphaFoldDB; A0A1D8Y7Y1; -.
DR STRING; 1904944.BIZ42_05435; -.
DR KEGG; slm:BIZ42_05435; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000177427; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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 PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF52; SENSOR PROTEIN KINASE PILS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AOX61687.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AOX61687.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..532
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 537 AA; 58399 MW; 2477C6DE69A01073 CRC64;
MSPSASLIDR IESIPRRELY FFALYRLLMA TVIGALLFSP LSGLVGTADH PRLATFVASG
YLAVAVLVLL FGRNERWLRT IVVWSVAADI IAATLLAHAL PGASAGISMS LLFNIAAAAT
LLPLSMGLGL AAAASAATAG EYLWKQIEGG DPTRTLAELA MFVTSYLAIA FISYQVGNRA
RMNQQLANQR GDEVANLFQI NELIIRRMRT GVIVVDGANR ITLANEAAST LLGDADGNSG
SGRLELGSAA PELSRRLLRW RNGWTNEEMP LQLSPDQPEV QPRFARLLAG SDLTLVFLDD
STVVSRRAES LTLSAMGRFS ASLAHEIRNP LAAINYAAQL LEESTDIGDT DRRLLQIINQ
QCQRTNGIVE SVLGLARRER ANPENVDLAA FVRRFVLEYK QGLSLETDSV EPIISETSVH
ALVDPRHLHQ ILTVLVHNAL KYGRVADEPA RVRLRVARQE RTAIIDVMDR GPGIPETVAS
QLFRPFFTTS EHGTGLGLYI ARELCRANQA RLEYVSVPAG GACFRLVLAG PHTMMAG
//