ID A0A1B9R2E2_9VIBR Unreviewed; 1143 AA.
AC A0A1B9R2E2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A6E14_04660 {ECO:0000313|EMBL:OCH78430.1};
OS Vibrio genomosp. F10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=723171 {ECO:0000313|EMBL:OCH78430.1, ECO:0000313|Proteomes:UP000093173};
RN [1] {ECO:0000313|Proteomes:UP000093173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9CSC122 {ECO:0000313|Proteomes:UP000093173};
RA Hehemann J.-H., Arevalo P., Datta M.S., Polz M.F.;
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: 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:OCH78430.1}.
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; MAJZ01000216; OCH78430.1; -; Genomic_DNA.
DR RefSeq; WP_017041522.1; NZ_MAJZ01000216.1.
DR AlphaFoldDB; A0A1B9R2E2; -.
DR Proteomes; UP000093173; 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 Kinase {ECO:0000313|EMBL:OCH78430.1};
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:UP000093173};
KW Transferase {ECO:0000313|EMBL:OCH78430.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..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..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..455
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 754..781
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; 127083 MW; F6F4E0CD2083C726 CRC64;
MQGWIVIPVS LAYLGILFLV AWYGDRQSHW LAKWRPWIYS LSIAVYCTSW TFYGTVGQAS
SNPWSFLPIY IAPIIVFTLG WRVLARLVLT AKREHITSIA DFIAARYGKS QGLAVVVTLI
AVAGILPYIA LQLRGITMGL EIVAPNLASD LGYQDRYVSW FVVGALAMFT MLFGTRHIDN
TEHHRGMMMA IAFESVIKLV AFLTVGFFII YLAWNQENID LVSVAKQTYQ SPNLPTLFIH
TLLTMVAIVC LPRQFHTMVV ENERAQDLHT ARWLFPLYLI LMGIFVLPIA WVGQSLLAGS
PADAYVISVP MSVGADNIAL LAFLGGTSAA SGMVIVSTIA LAIMVSNDLV MPLLLRRMRI
TGKNHRHFSG LLLIIRRALI LLLLIGAWGF YQALDTIHSL SAIGFLSFAA ITQFAPALIG
GMYWRTGNRK GVYVGLAFGF GIWLITLMSQ TGILAGDASN NALLWVITPP ELFTGWGVQS
SDWGMLLSVL INTFCYVFIS MVTRASLSER LQSASFVGTP LPESENQSLY QSRVTVAELE
MLASRFVGRT RVRNAFKQFW NQQHETLLPN QQAPSTLIRH TERVLAGVFG ASSAKLVLTS
ALQGKNMQLE EVATIVDEAS ELYDFSRGLL QGAIEHIGQG IAVVDRQLRL VAWNQRYLEL
FEFPAGLIQV GRPIADVIRH NAQNGLCGPG DPEGHVRRRV QHLEQGTRHT SSRIRPDGRV
IEVQGNPMPS GGFVMSFTDI TVFRDAEQAL KEANETLESR VLKRTQELER LNKQLVSATQ
RSEHESQSKS RFLAAVSHDL MQPLNAARLF ASSLTEVAKE QEVKGLSRHI ESALEAAEDL
IGDLLDISRL ESGKLDVNIH SFAIKDVLAN LDAEFSALAK QQQLSFKMIP SSLVVKSDPK
LLRRVVQNFL TNAFRYCPKG KVRLGVRRVG DDVRIEVWDN GIGIDENKQQ EIFEEFTRGS
QIRSDQGLGL GLAISKGIAH VLGHQISLRS WPKEGSVFSI TLNRASSEQI VEIKPTLLPV
SDLSHLKILC VDNEREILVG MESLLARWGC EIKTAEDLMQ SLKALEDNWV PDVIFSDYRL
DNGRTGLEVL QQCRLRLGDK FKGVIISADR TQDMLDGIKS NGFAFIPKPV KPLKLRAILN
QIK
//