ID W9GTR0_9PROT Unreviewed; 840 AA.
AC W9GTR0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, 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=N825_21365 {ECO:0000313|EMBL:EWY37139.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY37139.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY37139.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY37139.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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:EWY37139.1}.
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DR EMBL; AVFL01000030; EWY37139.1; -; Genomic_DNA.
DR AlphaFoldDB; W9GTR0; -.
DR STRING; 1385369.N825_21365; -.
DR PATRIC; fig|1385369.3.peg.5815; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000019486; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.
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; PF13426; PAS_9; 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; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EWY37139.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019486};
KW Transferase {ECO:0000313|EMBL:EWY37139.1}.
FT DOMAIN 197..250
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 327..397
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 470..693
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 721..837
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 595..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 772
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 840 AA; 90664 MW; EC0029B00DB862D6 CRC64;
MFGAGGLIAV GAAGLGLAAS GLVTDPVVLS GGVFALLAVG GVALAKRVST VEAAVQAEAE
GNADGERLTL SQAFQAGSMG RLITGRDGHV VRSNSAFRDL ISNAGVGSLD MFRHRFDHDP
EMSARFRGLV DAARNGVPAS AELALPSGGR GDGGPVIWYM VRVMPLSEEG AGNDGLVKWV
FEEISDRKQA EQRLRDEQAN LSDFMGSAPI GFYSVDQDGR FLYVNATLAE WLGCAPEDLM
DGSVRLRDVL ADSATAPGAA HSPFTGAENR GDVAMKGLSR NGVEGRRFQA SIIQTVVASG
DGRSLRTRSV VRDLTPEREW REKLHLSEQR FQSFFEEAPI GIALIDESGK LAECNQAFLT
MVGRPLPSIM GCPLAELFSP VERSTVLARL DEIKSGSDTI APFEVNLRVL GREKKMAQLY
ARRMAGATGN GVGSGSGMIL HFIDLTEQKS LEAQFAQSQK MQAIGQLAGG VAHDFNNLLT
AMIGFCDLLL LRHKPGDQSF SDIMQIKQNA NRAANLVRQL LAFSRQQTLQ PRVLNITDVL
AELSNLLRRL IGENIELKMT HGRELGLIKV DQGQLEQVII NLAVNARDAM SDGGRLSIQT
SNVSTDTPTR REHEEMPPGE YVVIEVGDTG TGIPKENLVR IFEPFFSTKE VGSGTGLGLS
TVYGIVRQTG GFIFVDSALG EGAKFTIYLP RHQAAKVASV TAEAESEARE RSAGDLTGTG
TILLVEDEDA VRVFSARALR NKGYQVLEAR SGEAALSVLN SETNRIDLLV SDVVMPHMDG
PTLIRHVRDK RPDMKVIFIS GYTEDKFRDQ IDAGEHIHFL PKPFSLKQLA GKVKEVLRDG
//