ID A0A432VPX3_9GAMM Unreviewed; 1157 AA.
AC A0A432VPX3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 13.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CWE06_11350 {ECO:0000313|EMBL:RUO18241.1};
OS Aliidiomarina haloalkalitolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=859059 {ECO:0000313|EMBL:RUO18241.1, ECO:0000313|Proteomes:UP000288212};
RN [1] {ECO:0000313|EMBL:RUO18241.1, ECO:0000313|Proteomes:UP000288212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK5 {ECO:0000313|EMBL:RUO18241.1,
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:RUO18241.1}.
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DR EMBL; PIPI01000010; RUO18241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432VPX3; -.
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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:RUO18241.1};
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 Transferase {ECO:0000313|EMBL:RUO18241.1};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..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..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 799..1009
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1030..1146
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 744..792
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1080
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1157 AA; 128176 MW; 948073AE86C3EBC7 CRC64;
MIWILIASAL GYIALLFLIA LWGERKHSLG YKISLHPWVY GLSLAIYCTT WTYYGAVGNA
IDGGWSFLPI LLGPVLLYVF GLPVVTKLVA VSKRQNITSI ADFIASRYGK NHKMALVVTV
IAAAAVIPYI ALQLKAVGIS FNVLSGMPPE VTGGSLKELI VALLMAAFAI VFGTRRLDVT
EYRSGMMLAI AFESTVKLVA LLGVAVFAWV AFRSDSVLTI TAQLESLQLS SSWGWQALNA
EFFIQLAMAA GAILCLPRQF HVTVVDNVHL SHLKTARWLF PVYLLLTSAA IAVLAITSTQ
LLGSYNGLPD ERSVFPLLIP YVNGQTWLAI VVYIGGISAA TAMVIVATLT LSTMISNDVV
MPVWLTREGQ KIPQPHRFSR RLIRVRRYAI VSVLVLGWAC YHLWFARLNL VSIGLLAFSV
VLQLLPAIIG GMYWRRGHAQ GVYWGLIAGM VTWLIAILLP LTQSPPEQTD TIITHGTLIA
MAANIAGYVV FSYLSVPALV DKIQATAFVQ PRSSYTNVGP QRLQQTRVAD LVLLMETFLG
AHRCEELLKS YQRHRQLDRD GIADAKFSDF AERAISGVLG AATARSLVNA AIENRQLNLE
EVVHFFDDTT QALQTQQSIM YSSLENLAQG ISVVDKDLRL VVWNRRYLEL FDYPDGMVQP
GRPIADLIRY NAERGECGVG EVEELVNKRL HYMQIGSPHR FIRRRSDGRV IEMVGNPLPN
GGFVTSFTDV TEHIETQQAL EDANIDLEAR IRSRTDEVRE INRELTEEID RRREIEIALQ
AAKAEAENAN ASKTRFLALA SHDILQPLNA ARLYLSAIDH ERLDGKNQGL IHKVDNALDS
TEHLLSALLS IAKMEQGAMQ PQLKHIDLNT ILGPLVPEYA VLAEQKDLQF KARLRNLTVY
TDPTYLRRIV QNFLSNAVKY TESGRVLLTV RKHGDHAELA VWDSGPGIPE QKHEEVFEAF
IRLHQGSISG VGLGLSVAKR MAEQLNCPLE IKSALGQGSR FSVLVPLGSA AMVIPRVRPE
RSNQAYDGLK ILCVDDEPEN LKALEALLHK WDCHPIQFTT PQEALTWAAE NPAPDGVLLD
YQLGEHGDGL TLWQALSDIW PNRVPGALVT AVRDPDLKAE TRKLGLQFLA KPVKPAQLKA
LMQHMQRQKE TQSCSGS
//
