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Database: UniProt
Entry: A0A1W1V4T1_9BACT
LinkDB: A0A1W1V4T1_9BACT
Original site: A0A1W1V4T1_9BACT 
ID   A0A1W1V4T1_9BACT        Unreviewed;       434 AA.
AC   A0A1W1V4T1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN00120144_1124 {ECO:0000313|EMBL:SMB87984.1};
OS   Hymenobacter roseosalivarius DSM 11622.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=645990 {ECO:0000313|EMBL:SMB87984.1, ECO:0000313|Proteomes:UP000192266};
RN   [1] {ECO:0000313|EMBL:SMB87984.1, ECO:0000313|Proteomes:UP000192266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11622 {ECO:0000313|EMBL:SMB87984.1,
RC   ECO:0000313|Proteomes:UP000192266};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWWW01000049; SMB87984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1V4T1; -.
DR   STRING; 645990.SAMN00120144_1124; -.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000192266; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SMB87984.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..104
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          109..154
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          226..434
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   434 AA;  48992 MW;  41617851662B08CA CRC64;
     MTLRVKFLLF VVIIHGVLIV LAAQLVRTNT VLFLVTEALL VVSIILTTQL YRGFVRPFQL
     IAAGTAAIRA KDFSLKFVPV GQREMDQLID VYNHMIDELR RERVAQHEKS LLLERLIQAS
     PAGILILDFD GKTEATNPAA ERFLGLTSQH LIGQPPAALP GDWGAFLSQL KPNEPQIVQL
     SGMQTYRASR GHFLDRGFTR YFILLEELTE ALIRQEKQAY EKLIRMMSHE INNSIGAINS
     ILQSFHHYAP QLTSPDQSDF REALDVSIAR NTHLANFIAG FANLVRLPAP TRRSCDVHAL
     LRATHRLMQV PSERRQVAWH WDLAPEPLRA DLDAQQLEQV LINITKNALE SIGDNGKIII
     RTRLHPPLLQ VEDDGPGIAP EAQRRLFTPF FSTKRDGQGI GLTLIRDILL QHGLRFSLET
     VEGRRTVFSV WLGE
//
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