ID F9RER4_VIBSN Unreviewed; 1143 AA.
AC F9RER4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VIBRN418_14103 {ECO:0000313|EMBL:EGU32195.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU32195.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU32195.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU32195.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
RL Submitted (AUG-2011) 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:EGU32195.1}.
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; AFWD01000064; EGU32195.1; -; Genomic_DNA.
DR RefSeq; WP_009386821.1; NZ_AFWD01000064.1.
DR AlphaFoldDB; F9RER4; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR Proteomes; UP000003627; 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; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000313|EMBL:EGU32195.1};
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 Transferase {ECO:0000313|EMBL:EGU32195.1};
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..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..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..450
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 MOD_RES 1077
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1143 AA; 126758 MW; 3A873D3AFDDD2640 CRC64;
MQGWLVIPVS LMYLGLLFLI AWYGDKQNKW LAKWRPWIYS LSIAVYCTSW TFYGTVGQAS
NNPWSFLPIY LAPILVFTFG WRVLARLILV AKREHITSIA DFIAARYGKS QGLAVVITLI
AVVGILPYIA LQLRGITMGL EVIAPELQSQ GQWGIFDVSW FVVIALAVFT MLFGTRHIDN
TEHHRGMMMA IAFESVIKLV AFLVVGCFIL FLALNRDDIV LMDVAAQTYQ SPNIATLVIH
TFLTMMAILC LPRQFHTMVV ENERAQDLHT ARWLFPLYLV LMGLFVLPVA WVGQALLGGV
SPDTYVISLP MSVGATDMAL LAFLGGTSAA SGMVIVSTIA LAIMVSNDLV MPLLLRRMKL
TQRDHRQFSG LLLVIRRGLI LLLLLGAWGF YQVLGNIHSL SAIGFLSFAA ISQFAPALLG
GMYWRQGNRK GVYVGLLFGF TLWLITLMSA TDMLAGDSHT NLLLWIIEPP QYLANMGIQN
SDWGIVLSLV LNTLCYVFVS SITRASLSER LQSASFIGSP LPESENISLY QSRVTVAELE
MLASRFVGRA RVRSAFQQFW GQQRETLMPN QQAPSSLIRH TERVLAGVFG ASSAKLVLTS
ALQGRNMQLE EVATIVDEAS ELYDFSRGLL QGAIEHIGQG IAVVDKQLRL VAWNQRYLEQ
FEFPVGLIQV GRPIADVIRH NAQQGLCGPG DPEDHVRRRI YHLEQGSRHT SSRVRADGRV
IEVQGNPMPG GGFVMSFTDI TVFRDAERAL KEANETLEER VLVRTQELER LNKQLVTATQ
RSEHESQSKS RFLAAVSHDL MQPLNAARLF ASSLSEVAKE SESKQLATHI ESALEAAEDL
IGDLLDISRL ESGKLDVNVH GFAINDVLSN LNAEFSALAK QQKIDFSLFP SQQLVQSDPK
LLRRVIQNFL TNAFRYSPQG KVLLGVRRAG EHVRIEVWDN GMGIDEDKQQ EIFEEFNRGS
QVRSDQGLGL GLAISKGIAN VLGHQIAMRS WPGKGSVFSI TLKRAKSVAP QLTVVSPQAV
SDLSHLNVLC VDNEPEILIG MDQLLARWGC NVRTATDIVG SLQAIDESWI PDVILSDYRL
DHGRTGLEVL QQCRLRLGDS FVGVIISADR TADMLDGIKS NGFSFIPKPV KPLKLRAILN
RSA
//
