ID A0A0S7YY70_9DELT Unreviewed; 704 AA.
AC A0A0S7YY70;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMJ54_00765 {ECO:0000313|EMBL:KPJ79020.1};
OS Deltaproteobacteria bacterium SG8_13.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ79020.1, ECO:0000313|Proteomes:UP000051346};
RN [1] {ECO:0000313|EMBL:KPJ79020.1, ECO:0000313|Proteomes:UP000051346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ79020.1};
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:KPJ79020.1}.
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DR EMBL; LJNK01000002; KPJ79020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YY70; -.
DR STRING; 1703398.AMJ54_00765; -.
DR PATRIC; fig|1703398.3.peg.1740; -.
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; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
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; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 1.
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; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..704
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006641006"
FT TRANSMEM 262..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 338..565
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 586..701
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 292..329
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 635
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 704 AA; 78326 MW; 8C4DD55E581443B2 CRC64;
MNIRLKSIAL AAAAAFSALM MASVQASASD TITVGVYQNM PLTFIEPQGT IKGFFVDVLE
HVAAKEGWKI KYDPDSWSEC LRKITNAETD LLGVIAYSVE RNKYLDYTYE SVLTEWGQIY
TSSDSGIESI LDLRDKKIAV LQADMHFLSL KRLMNQFGIQ CRYIEAFEYE DVLMLTELGI
CDAGLVSQFY GNQYERYYDI GKSAIILSPQ KLYWAAPKGR NSDILLTLDL HLRRLKKDEQ
SYYYQTLNKW FGVDTDSTYT VWIKWFGIGA GALLLLFLAA SLVLRSQVQV RTRELSAKTE
ALEAEIEQRE QAETERGQLE AKLQRARKME ALGTLAGGVA HDLNNILSGL VSYPELMLMD
LPQDSPLQRP IQTMKDSGEK AAAIVQDLLT LARRGVAVTE VVSLNHIVQQ YLTSFEFKKL
KTDCPTVRFE TDLSKGLLHI TGSPVHLSKT LMNLVSNAAE AIAGSGHVTI ETESRYVDRP
ISGYDDVEEG DYAVLSVTDD GIGISSDDTE RIFEPFYTKK VMGRSGSGLG MAVVWGTVKD
HQGYIDVQST KGQGTRFTLY FPVVREEMAL PKPKSTMADL TGNGELILVV DDVRQQREIA
SDMLEKLGYK VAAVGSGEEA VAYLRRHTAD LLVLDMIMEP GMDGLETYRQ VLAVHPGQKA
VIASGFSETK RVREAQRLGA GMYVKKPYTL EKIGQAVRQQ LNAG
//
