ID A0A193K9T7_9VIBR Unreviewed; 561 AA.
AC A0A193K9T7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A6E01_02400 {ECO:0000313|EMBL:ANO32138.1};
OS Vibrio breoganii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO32138.1, ECO:0000313|Proteomes:UP000092018};
RN [1] {ECO:0000313|EMBL:ANO32138.1, ECO:0000313|Proteomes:UP000092018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF50 {ECO:0000313|EMBL:ANO32138.1,
RC ECO:0000313|Proteomes:UP000092018};
RA Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C., Henschel A.,
RA Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale Resource
RT Partitioning in Marine Microbes.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016177; ANO32138.1; -; Genomic_DNA.
DR RefSeq; WP_065209485.1; NZ_MDAV01000039.1.
DR AlphaFoldDB; A0A193K9T7; -.
DR STRING; 553239.A6E01_02400; -.
DR KEGG; vbr:A6E01_02400; -.
DR eggNOG; COG3275; Bacteria.
DR Proteomes; UP000092018; Chromosome 1.
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; 1.10.1760.20; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PF06580; His_kinase; 1.
DR Pfam; PF15714; SpoVT_C; 1.
DR SMART; SM00065; GAF; 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:ANO32138.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ANO32138.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..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 134..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..361
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 561 AA; 62260 MW; 76C957AE007583DA CRC64;
MELILSLLQQ MCVYLMVAYT LSKTPLVIPL LNISERRSHK LICYVMFSLF CILGTYFGLQ
IDDAIANTRA IGAVLGGIFG GPLVGFAVGF TGGMHRYSMG GFTDLACAIS TTAEGLIGGL
VHLYMVKRGK TDRLFSAVIV FNVTLVAEIM QMLIIVIVAK PMEQAISLVE AIAIPMILAN
SLGAAFFISI LQDRRAILEK YSSAYSKRAL NIAERTVGVL SDGLNTQSAQ KIASIIQDET
HVGAVAITDK DKILAFEGIG SDHHRPNTPI SSEYTHTSIR EQRIIYLDGR KSPYQCSLSS
DCKLGSALVI PLIADDKVIG TIKLYEPRVK LFSSINMTMA KGIAELLSSQ ILNSEYQQKK
MLLSQAEIKL LHAQVNPHFL FNALNTISAI TRRDPHKARE LIQHLSQFFR GNLKRNTEFV
TLREELTHVN SYLTIEKSRF VDRLEVEIDI AEHLLDKMVP SFTLQPLVEN AIKHGVSNLL
ENGIVKIYSS PDATGDRITV EDNAGSYEPE NKDQTGLGMQ IVAKRLTNYF GEQYQLKIEC
APNNYTRMSF IIPSNHKDKH A
//
