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Database: UniProt
Entry: A0A0M0KQP5_9BACI
LinkDB: A0A0M0KQP5_9BACI
Original site: A0A0M0KQP5_9BACI 
ID   A0A0M0KQP5_9BACI        Unreviewed;       475 AA.
AC   A0A0M0KQP5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AMD01_19700 {ECO:0000313|EMBL:KOO41166.1};
OS   Priestia koreensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO41166.1, ECO:0000313|Proteomes:UP000037558};
RN   [1] {ECO:0000313|Proteomes:UP000037558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14210 dsm16467.";
RL   Submitted (AUG-2015) 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:KOO41166.1}.
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DR   EMBL; LILC01000030; KOO41166.1; -; Genomic_DNA.
DR   RefSeq; WP_053403151.1; NZ_LILC01000030.1.
DR   AlphaFoldDB; A0A0M0KQP5; -.
DR   STRING; 284581.AMD01_19700; -.
DR   PATRIC; fig|284581.3.peg.4329; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000037558; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 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; 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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037558};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          199..252
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          366..471
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   475 AA;  54374 MW;  D8F4FDACA5D64827 CRC64;
     MSIRNKLFIF IPLLVIFLNF IFFLIFYSGK QVQESYHVVT ERILLYKQIT DGSKHNLRTL
     NQHLTSQDDK SLQAFQREKL SLKELRSQLA DQENIGTSHT LMIQDLEHMI DSFVEEEEAT
     ISALQKGDLA QYTLHYAEAE KTSSFIREEG QNLVDAELSF YQPFYKNILR HTEVINRLGA
     ALFIMTTVVS IGLAIWLSRS ITNPINHLVQ AARRISHGEV SPDMPKGNDR DEIGILALAF
     QHMLKSLKEL NEKQLESVEK DRLVKELELK ALQNQINPHF LFNTLNALSK LAFIEGAEKT
     SDLTISVSNL LRYNLQKLDQ PVTLREEVEN VSEYFAIQKA RFRERITFQT VIEEEAMNHL
     VPCLTLQPII ENAFVHGIEG MEEGAVICLR IQKQEDTVKI SIEDNGVGMS EETKQSLLRM
     EQGAVPSTST GIGTVNVFKR LELFYETNNL VRIESKEGEG TLVMFHLPYT SMHEQ
//
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