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Database: UniProt
Entry: W9H452_9PROT
LinkDB: W9H452_9PROT
Original site: W9H452_9PROT 
ID   W9H452_9PROT            Unreviewed;       517 AA.
AC   W9H452;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=N825_33380 {ECO:0000313|EMBL:EWY40824.1};
OS   Skermanella stibiiresistens SB22.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Skermanella.
OX   NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY40824.1, ECO:0000313|Proteomes:UP000019486};
RN   [1] {ECO:0000313|EMBL:EWY40824.1, ECO:0000313|Proteomes:UP000019486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB22 {ECO:0000313|EMBL:EWY40824.1,
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:EWY40824.1}.
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DR   EMBL; AVFL01000006; EWY40824.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9H452; -.
DR   STRING; 1385369.N825_33380; -.
DR   PATRIC; fig|1385369.3.peg.2120; -.
DR   OrthoDB; 9808408at2; -.
DR   Proteomes; UP000019486; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd19410; HK9-like_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019486};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          274..509
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          102..139
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          229..256
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   517 AA;  57546 MW;  8C2F1A8D87EEE329 CRC64;
     MDREANETGP RAPREFRRFW RSFSNGRLFK LGGRRGELTW GFVLLLLIGT ASVLLVFANR
     EYGSLVTHTL EVRSRAFQLL TLVQDVETGQ RSYLLTGNPS YLERYREGAR ASLENLARLQ
     ETTTDNQQQQ NEIAVLRRTL ESRLDIAART IDLYQTGNAD GAMELVRTER GRVLMDGIRA
     SIDRIQAEEQ RLLKRREATA ETYGLLLLIA TLSGIALVIG IAAMSVIRVR RHTAALESLQ
     GELRAANENL EGIVAARVAE LNAANEEIQR FAYIVSHDLR APLVNVMGFT SELDVLRGQI
     VGFYETVAAK APELADAEVR IALEEDLPEA LRFIRTSTVK MDRLISAILR LSREGRRVLT
     PEPVEMREII EGIAGSLKHQ TEEQGVTVEI GGTPRLVTDR LAIEQIFSNL IENAIKYLDP
     ARPGHVIISG RNIGPEVRYE IVDNGRGIES KDFERIFDLF RRAGAQDRPG EGIGLAHVRA
     MVRRLGGSIT VDSQPGMGST FTVTLPSILS IKTLEPS
//
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