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Database: UniProt
Entry: A0A0V8J1K1_9BACI
LinkDB: A0A0V8J1K1_9BACI
Original site: A0A0V8J1K1_9BACI 
ID   A0A0V8J1K1_9BACI        Unreviewed;       531 AA.
AC   A0A0V8J1K1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   18-JUN-2025, entry version 43.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AS030_18670 {ECO:0000313|EMBL:KSU80977.1};
OS   Fictibacillus enclensis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Fictibacillus.
OX   NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU80977.1, ECO:0000313|Proteomes:UP000054099};
RN   [1] {ECO:0000313|EMBL:KSU80977.1, ECO:0000313|Proteomes:UP000054099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU80977.1,
RC   ECO:0000313|Proteomes:UP000054099};
RX   PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA   Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA   Ramana V.V., Shouche Y.S.;
RT   "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL   Antonie Van Leeuwenhoek 105:461-469(2014).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KSU80977.1}.
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DR   EMBL; LNQN01000006; KSU80977.1; -; Genomic_DNA.
DR   RefSeq; WP_061974502.1; NZ_FMAV01000004.1.
DR   AlphaFoldDB; A0A0V8J1K1; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000054099; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd18773; PDC1_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR43547:SF3; SENSOR PROTEIN CITS; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054099};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          263..324
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          423..528
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   531 AA;  59034 MW;  CF5AD44C9E499BA3 CRC64;
     MKAVKVSLQI KILGLVLLFG FFLIVLLTGY FSYKESNQIE ENRGRLALEL AKSISFMPSV
     IEAFDTDDPA KTIQPLAEKI RKSTGAEFIV VGNRQGIRYS HPVPSEIGKK MKGGDNKRAL
     QGKYYVSRAK GSLGPSLRGK APIYNKQGEI IGLVSVGFLL EDINEQITNN LQKVLVVSFL
     ALIVSIIGSF MLSRNIRKDT MGLEPYEIAA LYKEKNAVYH SVKEGILAIK KDGRITNMNQ
     PAKRLLNIEG SVRNMKVDGL FPSDYLYEVM QHGSPEPDKE MYWKGQTVIV NCTPLRNESG
     EITGVVASFR DKTEIEQMVN TLSEVKQYSD DLRSQTHEYT NKLYVLYGLL QLGEYEEAID
     MIKNETTLLQ LQHSVVFRQI QDTKVQAILL GKLAKASEKK IQFEIAPDST LEVLPQHIKL
     SNLIVILGNI IDNAFDAVSG MESPAVKLFV TDIGSDIIFE VEDNGTGIGE KEIPQLFNRG
     YTSKTGSKPR GYGLANADEA VKELNGIIEV HSQPENGTVF TVYLPKNNQG S
//
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