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Database: UniProt
Entry: A0A1L3MMB0_9BACI
LinkDB: A0A1L3MMB0_9BACI
Original site: A0A1L3MMB0_9BACI 
ID   A0A1L3MMB0_9BACI        Unreviewed;       480 AA.
AC   A0A1L3MMB0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A9C19_00980 {ECO:0000313|EMBL:APH03442.1};
OS   Bacillus weihaiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH03442.1, ECO:0000313|Proteomes:UP000181936};
RN   [1] {ECO:0000313|EMBL:APH03442.1, ECO:0000313|Proteomes:UP000181936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alg07 {ECO:0000313|EMBL:APH03442.1,
RC   ECO:0000313|Proteomes:UP000181936};
RX   PubMed=27901120; DOI=10.1038/srep38248;
RA   Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT   "Complete genome sequence and transcriptomic analysis of a novel marine
RT   strain Bacillus weihaiensis reveals the mechanism of brown algae
RT   degradation.";
RL   Sci. Rep. 6:38248-38248(2016).
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}.
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DR   EMBL; CP016020; APH03442.1; -; Genomic_DNA.
DR   RefSeq; WP_072578228.1; NZ_CP016020.1.
DR   AlphaFoldDB; A0A1L3MMB0; -.
DR   STRING; 1547283.A9C19_00980; -.
DR   KEGG; bwh:A9C19_00980; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000181936; Chromosome.
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:UP000181936};
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        177..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          276..476
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   480 AA;  55707 MW;  5530B5C63C0EC2C8 CRC64;
     MNKIRTKVLL YFLAFVLLFN LVSYSIYYSS SQIVSEYHSS FERFLLFNEI TQQSTQVYEK
     INAYVVEKDA MFIEEYTDIK KRLQENNQKL TAEAVTGINK QELEKYQRMI RNLLFESDVT
     IAAVQLHNVD QYTSHAKEVR NISSYILEST LQLLNLELAD YHMFYQEMTD RQHSFKWFTI
     NLFTSTLMFG LLAAVWFSRG LTNPLMKLSK AAKEVSEGKF DGPPISLKTN DEVKILSDSF
     EDMRNNIKKL ILEIKEKSEL DKLLKELELK HLQNQINPHF LFNTLNTISR MAYLEDATVT
     SRLIQSVSTL LRSSLGDINK TVSLREETKV VKEYFHIQKT RFAERIQFQT DIDESCLDVQ
     IPTLTLQPLV ENAFIHGVEE REEGGTIGLK IYRDPQKDQI IVEVSDNGKG MNDSTRQQIL
     SKQEIDLQEE HSGHSTGIGL RNVIKRLELV YKERVLDIES EENRGTTIKI KLPIKKEVIA
//
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