ID A0A257XAM5_9BACT Unreviewed; 618 AA.
AC A0A257XAM5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B7Z47_01450 {ECO:0000313|EMBL:OYW31308.1};
OS Chthoniobacter sp. 12-60-6.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=1970334 {ECO:0000313|EMBL:OYW31308.1, ECO:0000313|Proteomes:UP000216696};
RN [1] {ECO:0000313|EMBL:OYW31308.1, ECO:0000313|Proteomes:UP000216696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-60-6 {ECO:0000313|EMBL:OYW31308.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-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};
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:OYW31308.1}.
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DR EMBL; NCCH01000033; OYW31308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257XAM5; -.
DR Proteomes; UP000216696; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43047:SF5; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OYW31308.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:OYW31308.1}.
FT DOMAIN 9..73
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 127..179
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 204..254
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 248..301
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 325..375
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 393..613
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 618 AA; 68190 MW; CF80E42EE8CC8428 CRC64;
MNSQFDHLLL TETPDAVIIT TPDGKVVYWN TGAETVFGYT SAEAAGALVH DLIVAPERKE
EERLMLEKAV EGGFPTYEAI RRTKTGSLVY VAISGRLIRD AQNRIEYILS SQKDVTHLKV
LREAKLVEAK FSDLLESTPD AIIMANSAGR IVLANTQAEK LFGYSHGELL GQLVEVLLPA
RYRGGHVGHR SNYFDQPRTR TMGAGLELYG LRKDGVQFPV EISLSPLKTD EGTLVMSAIR
DISERKKAEQ KFRGLLESAP DAIVIANGDG DILLVNAQTE NLFGYPRAEL LGQKVEILVP
ERFRRKHPGH RDGFVGAPKT RAMGAGLDLF GLRKDGTEFP VEISLSPLET EDGTLVSSAI
RDISERRRIE QALHEKNVEL QQAAEAKNLF LANMSHELRT PLNGIIGFAE FLADGKPGAL
NAKQKEYLLD ILNSGQHLLQ LINDVLDLAK VEAGKMELVR EVFRLQAAVD EVRAVAKPIA
EKKHIRVSAK IAPDMECVTL DQQKFKQMLY NLLSNAIKFT DDGGVVDIVA ARHGEHQFKL
SIQDTGIGIR SEDIRRLFTE FEQLESGTSR HYEGTGLGLA LTRKLVELEG GSIEVESEVG
KGSTFTVVLP LITGKEEP
//