ID W1Q1F2_ABIDE Unreviewed; 387 AA.
AC W1Q1F2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GCWU000182_002005 {ECO:0000313|EMBL:ESK64818.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK64818.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK64818.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK64818.1,
RC ECO:0000313|Proteomes:UP000019050};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) 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:ESK64818.1}.
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DR EMBL; ACIN03000017; ESK64818.1; -; Genomic_DNA.
DR RefSeq; WP_023392598.1; NZ_KI535342.1.
DR AlphaFoldDB; W1Q1F2; -.
DR STRING; 592010.GCWU000182_002005; -.
DR GeneID; 84817011; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_3_9; -.
DR OrthoDB; 335833at2; -.
DR Proteomes; UP000019050; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF14; SENSOR HISTIDINE KINASE CSSS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ESK64818.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019050};
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 24..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..152
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 167..384
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 387 AA; 44734 MW; 7532CC1E1A4AE2CB CRC64;
MKDKDKKATQ PLSMRLTRSE RSELIVEAII TMSLIFFLYL SALLIYRQAI DYKLNFFGLD
TTLRHMLGLT RQQIIVSVYI FSLASCVVAI LVTNWRVKRR INQMKLAHIL DYLKYIAQGH
YEIRIPQTDL GEMDEVVSSI NHLVDSTVRA IEEERKIEKS KDELITNIGH DIRTPLTSVI
GYLGLIENQQ YHSQEELARY AHVAYRKAQQ MQSLVQDLFT YTATRQTTTE ISPVQVQVLR
FMEQLVADFE LSAREKTIEL RLDIRPKNLV ASFDVDKMAR VFHNLLSNAL KYGIGAHYIE
LLAYQEEDYI YFKVKNDGQP LDQSELEDIF QRSYRADQSR SANQPGTGLG LAIVRNIVEL
HHGRVYAEVE GKETIFTIEI PQKSPQQ
//
