ID A0A1C3EC01_9GAMM Unreviewed; 1148 AA.
AC A0A1C3EC01;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A8L45_19240 {ECO:0000313|EMBL:ODA30787.1};
OS Veronia pacifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Veronia.
OX NCBI_TaxID=1080227 {ECO:0000313|EMBL:ODA30787.1, ECO:0000313|Proteomes:UP000094936};
RN [1] {ECO:0000313|EMBL:ODA30787.1, ECO:0000313|Proteomes:UP000094936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 1920 {ECO:0000313|EMBL:ODA30787.1,
RC ECO:0000313|Proteomes:UP000094936};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (MAY-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:ODA30787.1}.
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DR EMBL; LYBM01000047; ODA30787.1; -; Genomic_DNA.
DR RefSeq; WP_068904984.1; NZ_LYBM01000047.1.
DR AlphaFoldDB; A0A1C3EC01; -.
DR STRING; 1080227.A8L45_19240; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000094936; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000313|EMBL:ODA30787.1};
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:UP000094936};
KW Transferase {ECO:0000313|EMBL:ODA30787.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 794..1005
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1031..1147
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1081
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1148 AA; 126833 MW; C877CFE547111381 CRC64;
MLQGWMVVLV SLLYLGVLFA IAWYGDRRPD WLSGWRPWIY SLSIAVYCTS WTFFGTVGQA
SSEPWSFLPI YLAPIIVFTF CWRFLARIIL ISKRENITSI ADFIAARYGK SQGLAVVITL
IAVIGILPYI ALQLRGIIMG LGVIAPEISI GLEQHKVAWL VCVSLAIFTV LFGSRHIDST
EHHRGLMMAI AFESIVKLLA FLLVGFFVVD LLLSVDINLP SVTETTVVGE PQWASLIVHT
ILTMAAIFCL PRQFHTMVVE NTHTDDLHTA RRVFPIYLLL MGFFVLPIAY AGQVLLPGEL
ADTYVLRLPQ STGSDWIALA AFLGGVSAAS GMVIVSTTAL STMVSNDLVL PLLLRRMRVS
DRSFIQLSDL LLNVRRGLII LLLIGAWGFY QLILEVPSLS AIGFLSFSAI AQFAPPLVAG
IYWRQANKKG VYAGLLAGFV IWLMTLMVQT GMLAGSPETN AVLWLLSPPD VFLLRDLSMA
DWGMVLSVML NAVCLILVSA VSRPSLAERL QVSSFVGNQV PEDDDSSLYY SRVTIGELEL
LASRFVGRKR MRNSLELYAR QRGEILNTNA QASTGLIRHT ERVLAGVFGT SSAKLVLSSA
LQGRNMQLEE IATIVDEASE LFDFNRGLLQ GAIEHISQGI SVVDRQLRLV AWNQRYIELF
RFPRDFIQVG RPIADVIRFN AERGLCGPGD IDQHVRKRVA FLKRGSRHTS SRVHQDGKVI
EVQGNPMPSG GFVMSFTDIT VFRNAESALK QSNEDLEARV TERTQELESL NTQLVSATLE
AEKASHSKSQ LLAAVSHDLM QPLNAARLFA ASLKEVAGDS EVTRISGHIH SALGAAEDLI
SDLLDISRLE SGKVKTRISE FALDDVFATL DAEFGVIADE QGISFRVRRT GLMVRSDRRL
LRRVLQNFLT NAFRYNPKGQ VLLGARRLNG HCRIEVWDNG PGIPPERQRD IFNEFTRIDH
EGADIGLGLG LAIAKGISLI LDHPLDLRSW QGKGTVFSIT APRILALSEL DTTSTKVRSN
DTDSAPLAGV RVLCVDNEKD ILAGMESLLS RWQCDIRIAR GLTDVEKLLV TDWKPQVVLS
DFHLSDTMTG LDVLHICRSK LGETFVGAVV TADKSPETRQ LITAEGFSQI AKPVKPLKLR
AIIQRGVN
//
