ID A0A0F6A1E5_9GAMM Unreviewed; 565 AA.
AC A0A0F6A1E5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RN22_05955 {ECO:0000313|EMBL:KKD61392.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61392.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD61392.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD61392.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-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:KKD61392.1}.
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DR EMBL; LASY01000024; KKD61392.1; -; Genomic_DNA.
DR RefSeq; WP_046303519.1; NZ_LASY01000024.1.
DR AlphaFoldDB; A0A0F6A1E5; -.
DR PATRIC; fig|1581149.3.peg.1739; -.
DR OrthoDB; 2514702at2; -.
DR Proteomes; UP000033732; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR34220:SF10; SENSOR HISTIDINE KINASE BTSS; 1.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF15714; SpoVT_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:KKD61392.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KKD61392.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..194
FT /note="Signal transduction histidine kinase 5TM receptor
FT LytS transmembrane region"
FT /evidence="ECO:0000259|Pfam:PF07694"
FT DOMAIN 366..444
FT /note="Signal transduction histidine kinase internal
FT region"
FT /evidence="ECO:0000259|Pfam:PF06580"
FT DOMAIN 464..554
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF02518"
SQ SEQUENCE 565 AA; 61918 MW; B1841FA029791E3D CRC64;
MELVISLLQQ MCVYLVLAYM LSKTPIVLPL LNISSRLSHR LICYVLFSGF CILGTYFGLQ
INDAIANTRA IGAVMGGLFG GPVVGFFVGL TGGIHRYSLG GFTDLACAIS TTAEGLIGGL
MHVYFVKRNR VSQLFSPVVV FGITFVAEVV QMAILLLVAK PFDQSYALVS TIAAPMIIAN
SCGAALFMSI LQDRKTIFEK YSASFSRRAL TIADRCVGIL HNGLNGESAG KIARIIYEET
QVGAVSITDK EKILAFVGIG DDHHLPETKI SSQNTLDAIE MNKIMYLDGA EKPYQCSLSA
ECKLGSALII PLRSGEEVVG TIKLYERKHK LFSTINMSMA EGIAQLLSSQ ILFSGYLQQK
SLLTQAEVKL LHAQVNPHFL FNALNTISAV VRRDADKARE LIQNLSQFFR SNLKQNVRSV
SLRDELDHVN AYLSIEKARF TDRLNVDIKI DDCLLDVQIP SFTLQPLVEN AIKHGVSNLL
EGGTVRIFSQ PYADGFSISV EDNAGCFTPP PENHQGLGLE IVTKRLEHQF GRDSSLKIES
EPDQFTRMTF IIPASEVSTG AKVGC
//