ID A0A0S7YSH0_9DELT Unreviewed; 590 AA.
AC A0A0S7YSH0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMJ54_06180 {ECO:0000313|EMBL:KPJ77762.1};
OS Deltaproteobacteria bacterium SG8_13.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ77762.1, ECO:0000313|Proteomes:UP000051346};
RN [1] {ECO:0000313|EMBL:KPJ77762.1, ECO:0000313|Proteomes:UP000051346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ77762.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ77762.1}.
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DR EMBL; LJNK01000017; KPJ77762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YSH0; -.
DR STRING; 1703398.AMJ54_06180; -.
DR PATRIC; fig|1703398.3.peg.1837; -.
DR Proteomes; UP000051346; 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; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR003660; HAMP_dom.
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; IPR000014; PAS.
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; 1.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..244
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 373..590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 590 AA; 65529 MW; B0F6146E3DEFD416 CRC64;
MRKKRRLVWH LFPSYLLITI FSLVAVTWYA TEALQRFYLN QTQQDLQARA HLLEKQIISL
LSPLDAEVVD AICKELGQLS ATRITVILPD GAVIGDSRDT PRFMDNHANR EEVVAALGGG
IGKSMRYSNT LQQRMMYVAV PLMKADRVVV VVRTSVSVSS LDEAMNSIRL KIALGVLVIA
LLAAGVSFYI SRRISQPIER IREGAQHFSS GNLAHRLPAV GVEEMAGLAE ALNRMAVQLD
DRLKTVVRQR NELEAVLSSM LEGVAAVDQN ELIIRMNQAA GRMFDCDPSD ATGRHIQEVI
RNLALQRFVL GALSSGKAVE DDFIVYRGGE RVLNVRCSPL FDASNRQIGT LLVISDVTQL
RHLENVRSDF VANVSHEIKT PLTAIKGFVE TLQQGSVDRR EEQERFLDIV LKHVNRLHAI
LEDLLSLSRI EQENDQNEIQ LENGSIKKVV QTAVQVCQPK AAEKNIEVRL DCPAEIATRI
DATLLEQALV NLIDNAINYS EQGSTVQVRA DRKDSEVIID ITDQGPGIHS RHLPRLFERF
YRIDKARSRK LGGTGLGLAI VKHIVQAHGG HVSVDSTLGK GSTFTIHLPA
//
