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Database: UniProt
Entry: A0A1D8Y7L9_9GAMM
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ID   A0A1D8Y7L9_9GAMM        Unreviewed;      1168 AA.
AC   A0A1D8Y7L9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BIZ42_04825 {ECO:0000313|EMBL:AOX61574.1};
OS   Stenotrophomonas sp. LM091.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX61574.1, ECO:0000313|Proteomes:UP000177427};
RN   [1] {ECO:0000313|EMBL:AOX61574.1, ECO:0000313|Proteomes:UP000177427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM091 {ECO:0000313|EMBL:AOX61574.1,
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; AOX61574.1; -; Genomic_DNA.
DR   RefSeq; WP_070425717.1; NZ_CP017483.1.
DR   AlphaFoldDB; A0A1D8Y7L9; -.
DR   STRING; 1904944.BIZ42_04825; -.
DR   KEGG; slm:BIZ42_04825; -.
DR   OrthoDB; 6053432at2; -.
DR   Proteomes; UP000177427; Chromosome.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF07494; Reg_prop; 1.
DR   Pfam; PF07495; Y_Y_Y; 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; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}.
FT   DOMAIN          809..1028
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1051..1165
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1101
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1168 AA;  125852 MW;  89A71DE07FFFF5AD CRC64;
     MGHRWAAVML GLALWLPVPV LAGDPVTAPW PRPLGPADAL PTAALRAVVE DRDGYLWFAS
     DDGLLRFDGH RFRAWRREQG LLDVDVRALH LDAQDQLWLA TASQGLLTLS ADRREIQSVP
     GNGAVVLPRI GVMQITSTPD GVVWVGTLDD GLFARQPDGR WQRVPLQLHG GPVRRVTALV
     TDRQGRLWIG TPAGALRRED HRFTQVPLQD DQGGDVRALW PDPDGGVWVR TPQGVYRWRD
     GELYQMPEGT AMPVLRSTAG DLWSAGATGL RLHARGQAPQ PVPLRGYAGA VMSTAAVSHA
     LEDRVGGLWW VGRGEGLWHL PARWRQFTLL AAARDGWPGL DGDHVLALAP SHGRRVWIAG
     DRGRLQRVDT VSGRSDLGID YRPDHLRAGT VAIAEDRRGQ VWVASGNTLS RYLPGSGGRR
     HWLLGVGGEA GRVDLQACGD GSLWLGRADR IQRRDADGVL QLSAAPHTLG LVPPSHGPQL
     LCDDDGRLWA TDRSGVKRWL PAQERFAVVE GAPRGEVGAI ARGEDGHYWI SSLGVLRRYC
     WDGQQLRKTH SFGPAHGYPR LLARALVVDA AGVAWAGDAR GLVRVDPHGG GVRHFGGDEG
     LPAQGVLPHG LVRTADGRLA AAVSEGGLLL IDPAGVGGPE RAPGLVIHAI TARRGKAQIT
     LPVGAGPVPL SGADRHVRVA ARLLSSGAPS HVQYRFRLQD HEAQWQESDA TGLRVFERLP
     VGLQTLEVQA RQGNGRWSPV RRVTLQVAPA WWQAPPARWA AAAAGLGAVW LWGWRFHVRR
     GRQRRWRWLR ARQGHAERAS VQRTRFLTTL GTRIRVPMTA VLGWSELLRR SPLPPGQRSR
     VNSLHHAGEH LLRLMDDALD LASIESGELQ LQPAPFVLQR MIEALHALLL PVAQGKALAL
     EWHSTLPASA CVIGDARRLR QILLNLLGNA LKFTAQGTVR LEAHGVHDGQ GIVLRVCDTG
     PGMTPAQCQR LFQRFEQADG AQTAARYGGS GLGLSISRDL AVAMGGDITV TSAPGQGTCF
     QVALPLPRGE LPTGIVAACA LPGPAAAGAL RVLVVYPSAV VAEVLLAMLA SLGHLPTHFP
     GADALPPTAA DGAAWDVIVV DPALWVDGER VGARLSRRWP GVPRVALTAR ADAAAQREAI
     AAGFELFLRL PVSRAALGDG LARCRRSA
//
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