ID B4SN91_STRM5 Unreviewed; 689 AA.
AC B4SN91;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Smal_1031 {ECO:0000313|EMBL:ACF50736.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50736.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF50736.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF50736.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) 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; CP001111; ACF50736.1; -; Genomic_DNA.
DR RefSeq; WP_012510349.1; NC_011071.1.
DR AlphaFoldDB; B4SN91; -.
DR STRING; 391008.Smal_1031; -.
DR KEGG; smt:Smal_1031; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_6; -.
DR OrthoDB; 9770473at2; -.
DR Proteomes; UP000001867; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
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; 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; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACF50736.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACF50736.1}.
FT DOMAIN 154..224
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 323..545
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 566..681
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 616
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 689 AA; 74540 MW; 52D757AD905E34CC CRC64;
MSDSGESRKV VRIVAPFGRD ADSIAAVLEG AGLATRIAGN LEELAEHLDD RTGLVVVTQE
ALVRGTDGML PALQQQPAWS DIPFILLRSA RSYRRSTREE LLPVAINVVE MDRPLGSMSL
ISAVQGALRA RDKQFLVRDQ MAALADGRAA LARSETELRL IADAMPVLIA FVDRSMCFRF
ANRAYESWFD LATGEVIGRH VREVIGESVW QQRRAAMERA LDGQAALFEI TWPHPLRGRR
DCEVRYSPRT DTDGRVDGFH VFVTDITAAK LALSNSQQHA HALEAMVAER TRELEAQMAA
REASEAALRQ SQKMEAIGQL TGGIAHDFNN MLTGILSALD IVRLRLEMGR VDDLERFLDT
ATTSAQRAAA LTQRLLAFSR RQSLDARPVE INTLLVSVQH LLHSTIGETV RLRTETCPVP
LHATLDANQF ESAVLNLAIN ARDAMPDGGE LILRTAEADV HAGQYPAVPA GHYAVVAVAD
TGAGMAPEVV ERAFEPFFTT KPIGKGTGLG MSMVYGFMQQ SGGHIAIESR LGEGTTISLF
IPLVEAAASE TAAAPAKAIR LGAGQSILVV EDDEQVRMLV TVVLEDLGYQ AQVVGDADAA
LPILTSDQCI DLLITDVGLP GLNGRQLAEI ARHSRPTLPV LFMTGYAEKA QERSSFLDAG
MAMIAKPFLL DEFSAAVRTA MPETAGGNP
//
