ID U3AA95_9VIBR Unreviewed; 1143 AA.
AC U3AA95;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VAZ01S_053_00400 {ECO:0000313|EMBL:GAD76821.1};
OS Vibrio azureus NBRC 104587.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219077 {ECO:0000313|EMBL:GAD76821.1, ECO:0000313|Proteomes:UP000016567};
RN [1] {ECO:0000313|EMBL:GAD76821.1, ECO:0000313|Proteomes:UP000016567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104587 {ECO:0000313|EMBL:GAD76821.1,
RC ECO:0000313|Proteomes:UP000016567};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio azureus NBRC 104587.";
RL Submitted (SEP-2013) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434}.
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:GAD76821.1}.
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DR EMBL; BATL01000053; GAD76821.1; -; Genomic_DNA.
DR RefSeq; WP_021710568.1; NZ_BATL01000053.1.
DR AlphaFoldDB; U3AA95; -.
DR STRING; 1219077.VAZ01S_053_00400; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000016567; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd10322; SLC5sbd; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000016567};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 795..1006
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1027..1143
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 743..774
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1077
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1143 AA; 126983 MW; 3990D0B3D1523586 CRC64;
MQGWLVVPVS LVYLGVLFLI AWYGDRNKQW LSGWRPWIYS LSIAVYCTSW TFYGTVGQAS
VNPWSFLPIY IAPILVFTIG WRVLARLILI AKREHITSIA DFIAARYGKS QGLAVVVTLI
AVAGILPYIA LQLRGITMGL EMIAPELVNH EQYQEGRISL FVVGAMAMFT MLFGTRHIDT
TEHHRGMMMA IAFESVLKLV AFLVVGVFIV WLAFNTDSIN LAEVATQTYQ SPNVATLMIH
IVLTALAIVC LPRQFHTMVV ENERPQDLHV ARWLFPLYLV LMGAFVLPIA WVGQSLLAPD
LAENYVISVP MAVGADHIAL LAFLGGTSAA SGMVIVSTIA LAIMVSNDLV MPLILRRFKL
SQHSHHDISD LLLRIRRGLI LLLLLGAWLV YQALDGIHSL STIGFLSFAA ITQFAPSLIG
GMYWRQGNKK GVYFGLFVGF TLWLITLLNQ ANMLVGEAEN NGLIWLITPP EWLAGFDIAC
SDWGMILSVG ANALCFIIVS LMTRASVSER LQSASFIGIG LAESENISLY QSRVTVNELE
MLASRFVGRE RMKSAFQTYW KEHGQILQSS QQAPSSLIRH TERVLAGVFG ASSSKLVLTS
ALQGKNMRLE EVATIVDEAS ELYDFSRGLL QGAIEHIGQG IAVVDKQLRL VAWNQRYLEL
FVFPPGLIQV GRPIAEVIRH NAEQGLCGPG DPEQHVRRRV EHLEKGTRHT SSRIRPDGRV
IEVQGNPMPG GGFVMSFTDI TVFRQAEQTL KEANETLEER VQVRTHELEA LNKQLVIATQ
RSEQESQSKS RFLAAVSHDL MQPLNAARLF ASSLSEVAKD GEVHRLSSHI ESALGAAEDL
IGDLLDISRL ESGKLDVHAY GFAINDVLAN LHAEFSALAK QQNIQFSMVS SSLMVKSDPK
LLRRVVQNFL TNAFRYAPKG KVVLGVRRIK GQVRIDVWDN GMGIEQEKQQ EIFEEFSRGT
QVRSDQGLGL GLAISKGIAQ VLGHQISMRS WFGQGSVFSI VLDKAEKIQL ELIQESKRES
SNVSHLRVLC VDNEPDILVG MDNLLSRWGC DTRLAGDIVE SLKMIDDEWI PDVIFSDYRL
DDGRTGLEVL QQCRLRLGHR FKGVIISADR THEVVDGIKA NGFDFVAKPV KPLKLRALLN
QIV
//
