ID Q0F007_9PROT Unreviewed; 989 AA.
AC Q0F007;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SPV1_09288 {ECO:0000313|EMBL:EAU54877.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU54877.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU54877.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU54877.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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:EAU54877.1}.
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DR EMBL; AATS01000005; EAU54877.1; -; Genomic_DNA.
DR RefSeq; WP_009849378.1; NZ_DS022294.1.
DR AlphaFoldDB; Q0F007; -.
DR STRING; 314344.AL013_11395; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3614; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_62_0; -.
DR InParanoid; Q0F007; -.
DR OrthoDB; 9813903at2; -.
DR Proteomes; UP000005297; 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; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAU54877.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005297};
KW Transferase {ECO:0000313|EMBL:EAU54877.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 69..305
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 363..435
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 439..492
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 489..535
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 560..614
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 627..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 872..987
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 923
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 989 AA; 110612 MW; 649EE0133CBE59C1 CRC64;
MKKALLATLL MSLLVAGVIF YSWQLLQAGQ QQSLQSKFHV DIAEVKTEID EHMATYEQVL
RGARSLFLAS DKVTRQEWHS YVTTLELHKH YPGIQGVGYA VSIAPANLTK NEQQMHSEGF
PDYHVWPAGK RERYSAITYL EPFDWRNQRA FGYDMFSEPT RHEAMQRACD TGNAALSGKV
LLVQETNEEP QAGSLLYLPL YRKQAPLDTV QQRRQALIGW IYSPYRMENM IRGMLDNRDF
KGLRLRIYDV DSTIQKTPDS AHPDIDPAAL LYDSAGTSSK PVSDDAILAH YTLRMETAGR
TWLLDFDALP AYAEVIGLRS LHKEMSAMLL IGLLLILLTW NLFNTQRKAS LLAHDLTTSL
RQSEERWSFA LEGSGDGVWD WDIEAGKVFF SPRFKQLLGL AENELGNDIE EWRQRVHPDD
IAEVNDAINR HLNGETPEYS CEHRLRHNSG DYIWVLGRGK VTSRSEDGRP LRLVGTKSDI
SERRQTEESV HLLSQSVHQS GEAVIMTNAE GVIEYVNPAF TTITGYSAGE AIGQTSRLLK
SGVQNQEFYA NMWATISSGR SWRGRIVDQK NDGTNYPAML TISPITGKNG AITHYVGVQQ
DLHEYEDMEA RFHQAQKMEA IGTLIGGIAH DFNNTLAGIT GSIFLARKQV QENPELLERL
ETVDKLSFRA AAMIKQLLTF SRRNKAEMVP LAINSFLKET IKLQRISTRE DIELKSVIVD
HDLTVSGDIN LLQQVLVNLL NNARDAVQDR PDPRIEVKLE RYSAAPAVLA NHPELIARDY
ACISISDNGR GISPENIDHI FDPFFTTKGV GKGTGLGLSM AYGAVRQHNG VITVDSQPEQ
GSSFRIYLPL IEVSTATVDE TTVGVTMGLG QTVLLVDDHQ ELLDTNRKLL ESLNYLVLTA
SDGEEAVGIY SARRNEIELV ILDVVMPKMG GTEACKAIRE INPQARVLFA TGYDNAGMQQ
DETVADIPVI NKPFSAAKLS TIIHRLLST
//
