ID A0A1L8QSA6_9ENTE Unreviewed; 600 AA.
AC A0A1L8QSA6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RU93_GL002170 {ECO:0000313|EMBL:OJG10391.1};
OS Enterococcus aquimarinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=328396 {ECO:0000313|EMBL:OJG10391.1, ECO:0000313|Proteomes:UP000182149};
RN [1] {ECO:0000313|EMBL:OJG10391.1, ECO:0000313|Proteomes:UP000182149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17690 {ECO:0000313|EMBL:OJG10391.1,
RC ECO:0000313|Proteomes:UP000182149};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OJG10391.1}.
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DR EMBL; JXKD01000008; OJG10391.1; -; Genomic_DNA.
DR RefSeq; WP_071874871.1; NZ_JXKD01000008.1.
DR AlphaFoldDB; A0A1L8QSA6; -.
DR STRING; 328396.RU93_GL002170; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000182149; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OJG10391.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000182149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..378
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 485..594
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 600 AA; 68652 MW; 38D30D9E28E585F4 CRC64;
MKEKITRFVT AITHFFYRKG LQFTLLSTFT LVSVSAILLI TAGYMRQFSL TTEQMTRTSS
MEMLDQVNLN LDDYIHRLMG VSNTVYYKIL KDGDISKNQS AINRELSLLF SANESILSTI
AVFKNDGTLV NSAPINQLKA DANPLEESWF IEANQQIENV HFSKPTVDNL FLPMNNTYHW
VVSLSRSVEL MNDGVVERGV LLVNMNFSGM EKISLNANFG SKGYVYLMTP DGQLIYHPRQ
QLINSGLMLE NTHQAANYSE GSHNEVFQDE KRIVTVKTMG YTGWKIVGVT PVSEMRATLF
QNQLLLWSIA IIVSLFILSI NLLISKRVTN PLRQLEIAVS RMEQDIYDID IPVEGSYEIQ
HLSKTLMTMA YTMQRLMKDI VTQQEQMREK EMNALQQQIN PHFLYNTLDS TIWMIESGRY
EGAITMITAL AKFFRISLSK GKNIISLADE LSHVKSYLMI QEIRYKNKFE YHLSVDPSIE
NAATIKLIVQ PLVENAIYHG MDYMYEEGEI QIRAYRFKED IYIDIEDNGP GMTPEQLRQL
KEGTPTTTRK KGSGIGYSNV EERIKLFYGK AYGLEVYSEP DEGTLIRIHL PFQPLQEGGD
//
