GenomeNet

Database: UniProt
Entry: A0A0Q9KBM6_9BACL
LinkDB: A0A0Q9KBM6_9BACL
Original site: A0A0Q9KBM6_9BACL 
ID   A0A0Q9KBM6_9BACL        Unreviewed;       487 AA.
AC   A0A0Q9KBM6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASG81_21690 {ECO:0000313|EMBL:KRE35199.1};
OS   Paenibacillus sp. Soil522.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE35199.1, ECO:0000313|Proteomes:UP000051180};
RN   [1] {ECO:0000313|Proteomes:UP000051180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE35199.1, ECO:0000313|Proteomes:UP000051180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil522 {ECO:0000313|EMBL:KRE35199.1,
RC   ECO:0000313|Proteomes:UP000051180};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRE35199.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMRV01000066; KRE35199.1; -; Genomic_DNA.
DR   RefSeq; WP_056639145.1; NZ_LMRV01000066.1.
DR   AlphaFoldDB; A0A0Q9KBM6; -.
DR   STRING; 1736388.ASG81_21690; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000051180; 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; 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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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   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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..255
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          279..474
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   487 AA;  55171 MW;  C9134911EF71A792 CRC64;
     MTIRTKLLIF IPLLVLLVNF VTFFLFQSGK LVQQSYNQMM DRLLLYKQSS QTVEGNLGAL
     HNYLLNPDDS NNELFKQSRN KLMELRALLD DHSNASLRSS AVTSYNHMLD SFLEQEQAAF
     AAVTEETSRA SLAHYEKAEK IASFIRENGQ QLVDMELGIY QPIYKQIQAE NERMYLLGAA
     VFITNTLMSI LLAIWISRSI TGPVSRLVSR ARQISKGQLH QSDRQNRSSD RSSDELGLLS
     GAFEQMSSDL LVLIEKDKES LKKDKLVKEL ELQALQSQIN PHFLFNTLNV LSKLALLEGA
     EKTSDLIVSM SNLLRYNLRN LEQPVTLKDE VEHVKEYFII QQARFRDRIR LEMEIDQSAL
     QQPIPALTLQ PIIENAFLHG IESMEQGAVI RLEISQSTTG VRISLSDNGS GMTDEVRKSL
     LRLESGSDKK KSTGLGTKNV FKRLQLFYGV NELVDIESEL GKGTKVTIRI PPRKEGERIH
     VPTVDRG
//
DBGET integrated database retrieval system