ID A0A0Q7AGH8_9BURK Unreviewed; 485 AA.
AC A0A0Q7AGH8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC76_22510 {ECO:0000313|EMBL:KQW35160.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW35160.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW35160.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW35160.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW35160.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW35160.1,
RC ECO:0000313|Proteomes:UP000051611};
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 -!- 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:KQW35160.1}.
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DR EMBL; LMDS01000007; KQW35160.1; -; Genomic_DNA.
DR RefSeq; WP_056472295.1; NZ_LMDS01000007.1.
DR AlphaFoldDB; A0A0Q7AGH8; -.
DR STRING; 1736528.ASC76_22510; -.
DR OrthoDB; 2514702at2; -.
DR Proteomes; UP000051611; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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:SF9; HISTIDINE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KQW35160.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611};
KW Transferase {ECO:0000313|EMBL:KQW35160.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 384..477
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 85..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52250 MW; DDDBD2492C37B073 CRC64;
MSDFATTVAS TWKTVSATAV RLFHQYGNWL VGISWWRFGA FALLLLILTS ILQKLPPFRT
SWSEIVEEIP TVTVPPIPPI PPIKVPKIRI ESPTTPSNPA SGGQDDDVLI SIDGKGVRIT
SRSAPAAASA PASGAASAAS PAPDPASAAS TAADAGSSIQ IALPGATRET IREAVRAARE
AAREATQEAR QQAEEARREA QEAIEEAQRD AEEARREAQE ARKVKRTRVV HLGDSLTDLA
FFWIVASALL KITYKGRMQA EVKAAEATET AESEQLKRQV VEARMAAMQA QVEPHFLFNT
LASIDHLIET DPPRASQMQK NLIALLRASM PTMRENHPTA HNLGREMAVI RPYLEILKVR
MEDRLQTEIA VPDGLLSADF PSMMIQSLVE NAIKHGLEPK AEGGKLTVRA EIVHGKLAVT
VADTGLGFGR AATAGTGVGL NNIRERLQLL YGSKASMTVA ENSPSGTVVT LTVPYQAQTR
EGESA
//
