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Database: UniProt
Entry: A0A257XAM5_9BACT
LinkDB: A0A257XAM5_9BACT
Original site: A0A257XAM5_9BACT 
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
//
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