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Database: UniProt
Entry: W9GTR0_9PROT
LinkDB: W9GTR0_9PROT
Original site: W9GTR0_9PROT 
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
//
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