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Database: UniProt
Entry: A0A432VR99_9GAMM
LinkDB: A0A432VR99_9GAMM
Original site: A0A432VR99_9GAMM 
ID   A0A432VR99_9GAMM        Unreviewed;      1139 AA.
AC   A0A432VR99;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 14.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CWE06_09595 {ECO:0000313|EMBL:RUO18842.1};
OS   Aliidiomarina haloalkalitolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=859059 {ECO:0000313|EMBL:RUO18842.1, ECO:0000313|Proteomes:UP000288212};
RN   [1] {ECO:0000313|EMBL:RUO18842.1, ECO:0000313|Proteomes:UP000288212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK5 {ECO:0000313|EMBL:RUO18842.1,
RC   ECO:0000313|Proteomes:UP000288212};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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}.
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:RUO18842.1}.
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DR   EMBL; PIPI01000007; RUO18842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432VR99; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000288212; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000288212};
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..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..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        151..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          783..998
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1023..1136
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          728..776
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1070
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1139 AA;  126803 MW;  F14ECC7021E48EC6 CRC64;
     MLPVSVVLIT AILYLLIVFS IAARGEKRAH GDRPQPWRYT LALGVHCTTW AFYGTVTQTV
     HYGWWFAPTY LGGILFFLFA HRLMLHILTV VKQQNFTSIA DLIGARYGKS QFVSAFVALI
     ALVALVPYIA LQLRAITASF AAITGVDAEQ APWFVDVSAG VALVMMVFAI LFGARKLSLS
     EKHPGLMDAV AFESVVKLVA FMLIGLFCVY QLFDGFADVL IAAAANTVTQ EILGGKPQGL
     YIYLTHMLLG ALAMLVLPRQ FQVNFIENNH ADELKTARWG FPLYLFAINF FILPIALVGG
     LLVPEQRFDD MFVLAIPVLT ERPDISLIAF VGGLAAATSM VMMATLALSI MMSNDVFTPL
     WLRFNKLRVQ ELKLSADGVL NIRRLTIILI IVLAYLYHEA TESGVPLVSN GLIAMALLAQ
     LGPALIGGMV WQKGSRAGGI AALSAGTLLW TILLLIPSLR PSTSLTDIAI SHSVLISLGV
     NLLLYIVVSR LWPDSAPVQR QAGRFVNPDQ QDIAGAQARH VTWGRLRSVL ARFIDDREVR
     RLDDRLGMTI AVAPADSWVP AAVLQRIERE LAGAVGSAAS HLILHSLARK SPVSVDTVAD
     WASEATKLYR FNRELLQASV ENIPQGISVI DKDLRLVAWN RRYLEIFEYP DGFIHAGMPV
     VELLRFNAER GLFGQPDTDI QREINKRLSY LRQGSSYRYQ RKQHDGQIIE LQGSPMPDGG
     FVTTYTDITE LVTAQDELQR INQELEQRVA ERTRELTDTN QQLQQAKRAE EEAHQSKSRF
     FAAAGHDLMQ PFNAASLFCE MLQQRLAQAN LPDDHELARQ IQQSLNHAET LLTMLLEMTK
     LDSGTLKPEF SVVPLNDILR PLQESFKVMA HEQGLEFRVR PSRALIRTDK RLLIRVIQNL
     LANAIRYTEK GRVLCGVRRR SARLIELQIW DTGIGIPADK QTEIFKEFHQ LHQQSEHPGL
     GLGLAIVERM CRLLAIPVTV RSEEGRGTCF SLQLPVSGWQ QGQQTAEASS ELLNNQRILA
     GKRVLVLDNE ASLREAIGKL LQQWGADVVL CHSPADALSV TDKADLLVVD YHLDNQETGI
     AAIVALREHW QKHIPAILIT ADPDEGIREE VVQVGAMFLP KPLKQAPLLR ILKRLWPQM
//
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