ID K2DUM7_9BACT Unreviewed; 756 AA.
AC K2DUM7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, 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};
DE Flags: Fragment;
GN ORFNames=ACD_23C00904G0001 {ECO:0000313|EMBL:EKD97473.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD97473.1};
RN [1] {ECO:0000313|EMBL:EKD97473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD97473.1}.
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DR EMBL; AMFJ01009442; EKD97473.1; -; Genomic_DNA.
DR AlphaFoldDB; K2DUM7; -.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
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 NCBIfam; TIGR00229; sensory_box; 3.
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; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 81..144
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 141..193
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 212..266
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 267..312
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 563..756
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 250..277
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD97473.1"
FT NON_TER 756
FT /evidence="ECO:0000313|EMBL:EKD97473.1"
SQ SEQUENCE 756 AA; 84761 MW; C4060F228BAA8259 CRC64;
AAKDCAAKFA HSLQEQSARE HFYRSVLDSL PQRLFWKDRD SVFRGCNLSG ARALNLSSSS
EIAGKTDYDF YHDRKEADYL RTIDEQVMDS GQASFHTEVS SRERTTWLDV SKVPLRDMDG
EIYGLLVNYE DVSALKKSEM ALHKFRRAVE QSPSSIFIAD TAGNIEYANP SFFNTYGCER
HEVLGMNMDR LRPGLVSPEG YSGMLRAASS GENWSGELAK HSSDGEICWQ ACSFSPIFDE
SGNIIHFLSI ENDITERKRM EEALAENEAR LREITSTVGE GIYVVDTDNL VSFVNPAAAK
LFGCSEQEVL GQDACNLCGC FLQNDQHGED VEPGCLLDGI QQTCNVVYSD NEYFIRGDGI
QFPVSAIATP ILRDGSYAGA VVAFHDITEQ KFTQRLLNDT LRELRAVLDN AQIGVAYLRE
GKFFWINKHM EQMFGYVVGD LIGEPMETIY AIGENGSDGE GSKGFDFLAD GGVYETERLM
RRCTGKTFWC HQRGVAIDPD NPGKGSIWIM LDIDRLKTTE SNLKTLNETL AQRVEEETQK
TLERERLFIQ QGRNAAMGEM IGNIAHQWRQ PLSTLGLVVQ NIQADFQEKS LSASVLEEYV
ETATRAIQRM SCTIDDFRDF FRPNRAKERF SIYQSIYGTL QLLDAMLKNN GIAIRLTGDQ
GLKALGHPNE FSQVALNFLV NAKDALVDRK VPQGRIDIEL AGYDGWGVVT IRDNAGGIQD
EELEKIFDPY FTTKQNGTGI GLHMNKTIIE THMNGR
//
