ID M5CMU1_STEMA Unreviewed; 799 AA.
AC M5CMU1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SMSKK35_1640 {ECO:0000313|EMBL:CCP11678.1};
OS Stenotrophomonas maltophilia SKK35.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=1118156 {ECO:0000313|EMBL:CCP11678.1, ECO:0000313|Proteomes:UP000012178};
RN [1] {ECO:0000313|EMBL:CCP11678.1, ECO:0000313|Proteomes:UP000012178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKK35 {ECO:0000313|EMBL:CCP11678.1,
RC ECO:0000313|Proteomes:UP000012178};
RA Linke B., Adamek M., Schwartz T.;
RT "Stenotrophomonas maltophilia SKK35 and RA8 genome sequencing: analysis and
RT comparison of viurlence genes.";
RL Submitted (JUL-2012) 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:CCP11678.1}.
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DR EMBL; CALN01000778; CCP11678.1; -; Genomic_DNA.
DR AlphaFoldDB; M5CMU1; -.
DR Proteomes; UP000012178; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
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; 2.
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; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCP11678.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:CCP11678.1}.
FT DOMAIN 12..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 146..216
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 218..270
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 429..656
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 679..794
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 63
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 730
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 799 AA; 87455 MW; BF96D43F554A4840 CRC64;
MHDGSRRSER LRILMLEDSA LDAELITAQL QRAGLDFEAE RVWSRNAFIE AIDHRAFDVI
LADHVLPGFD GDAALALARE RIPHTPFIFV SGTLTEDLAV QALTRGARDY VVKQRLQRLP
DAIRRARQEA RERTQLADAQ AALNDSQAQL QQVTDAVPAL IAQLDKEHRY RFANRAFLDW
HGISLAELLG RSARDVSGIS AFEHALPSLQ QVLRGERSSF QVELAHRSGE SRFVQMDCVP
ERGPDGEVVG YICLGSDVSG LKQAELALRE DNQLLERQVQ ARTTELRASK RRLQAIFESS
FQHQVLLDLA GQVVDANIAS LAAVLADKPE VMGQRFGQSP WFAGTDGVGE TVDRAVADAA
KGHNSLHALD LELPTGRRSF DFSFRPLLDA EGAVTAVVSE AVETTARLQA EHALRQSQKI
EAVGQLTGGI AHDFNNILTV ISGNVEHAML LSERAGEPGA MVGRALDNAL KGVGRAASLT
QRLLAFARRQ PLHSQAANLN ERLLDMHDML QRALGELVQL DIRVAEDIWC IEIDVSQLEA
SVLNLAVNAR DAMPHGGRLI IEVDNSHLDH DYTALFPDAT PGEYVMLRVR DNGHGMDAAT
LARVFEPFFT TKQVGRGTGL GLSMVHGFVK QSGGHVLIDS VEGGGTSITM MFPRSTLALP
CEGTAPQTGL AGYSPREETI LVAEDNDDVR AHTVDALRML GYRVLEAHDG PSALRLLERP
DTTVDLLFSD VVMPGMSGWE LVREVRERWP DVAVLFTSGY PRDHDAVGSQ GRAVALLPKP
FTRSDLAQAV RTALEAALH
//
