ID I9CCU2_9SPHN Unreviewed; 1105 AA.
AC I9CCU2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=WSK_0210 {ECO:0000313|EMBL:EIZ81265.1};
OS Novosphingobium sp. Rr 2-17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ81265.1, ECO:0000313|Proteomes:UP000004732};
RN [1] {ECO:0000313|EMBL:EIZ81265.1, ECO:0000313|Proteomes:UP000004732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX PubMed=22933764; DOI=10.1128/JB.01159-12;
RA Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL J. Bacteriol. 194:5137-5138(2012).
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:EIZ81265.1}.
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DR EMBL; AKFJ01000005; EIZ81265.1; -; Genomic_DNA.
DR RefSeq; WP_008993176.1; NZ_AKFJ01000005.1.
DR AlphaFoldDB; I9CCU2; -.
DR PATRIC; fig|555793.3.peg.206; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000004732; 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 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 Kinase {ECO:0000313|EMBL:EIZ81265.1};
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:UP000004732};
KW Transferase {ECO:0000313|EMBL:EIZ81265.1};
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..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 760..969
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 990..1102
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1037
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1105 AA; 119277 MW; 405CF2E2529CA413 CRC64;
MSMPWIMALI YVAMMFAGTA LAHRYRQALH NSSWRIYAYT LAFAVYCTSW TYFGAVGSAA
TGGWDFLPIY LGPILLMALG GRFLRRLNVE VHKEGATSIS DFIAARFGKS RSVAALVTMI
ALFGTIPYIA LQLRSVALSF ALVSGTPEST GPLLVAAVVL AIFAIVFGAR RYQVSGQNEA
ILFAIAFESV LKLGAILLVS GLAVWLLWTI PDRQALTSLE HFRGRFALDT LDADFLVTML
VSVMAIVCLP RHFFISVTQA RHPDDILRAR WGFIAYLVIT VLAVLPIAGA GVATLDRGAM
PDLFVISLPQ QFGFDRLTLF VFLGGISAAV AMVVTETVAI SSMISNDLFA PILLRRSTRE
VHLGEQLLWI RRSTIIGLMA AAAGYAMLTP SATQLASVGL IAFVAMAQCT PALIFAVYRT
DNDALAAKGS LMVGFLLWFV LLFLPTISGN HIGEDARDMI PFAAFEHLSP VTSGALISLS
GNLLAYMLLA ARKVGKEGIG KVHIRHRGVS SISTVAGLVD LVTRFVGMEL ATEAFGPDSD
RARPIDRASV RTAERLIGSV VGVPSARAIM ASAISGQGMG LADVTQMLDA SGQSLHFSQG
LLAATLENID IGVSAVDRDL RLIAWNGRYL ELFTYPPGLV RIGVPIAELI RYNAERGDCG
PGEVDSHVAR RLDHMRSRQQ HSFERYRADG RVIKTVGGPM PDGGYVMSFT DITMEAQARA
ATETARKNLE SAVAERTAEL SEVNDKLARA MRDKTRFLAA ASHDLLQPLH AAMLFSAALR
RRLEPPEQAI LARLDRSIEA ANDLLRALLD ISKLDAGGVQ IAPDRFAVRP LLVDLAESFQ
PLAAEKGLRL RIGPSDGWVE CDRTLLRSIM QNFLSNAIRY TEQGGVIIAA RRRGARIQLA
VYDSGIGIPP DKLTDIFREF ERLGQAAETG IGLGLAIVER SAPLVGGTIT VRSWPGKGSV
FSISLPRVAQ AAVPPKPTVD LANSSGVSRH LLVVDDDPTN RDAMRLVLDG LGHRCITAAD
EQEALDCAGV FDGALIDFHL GNGRNGIDLI DALRVKRPCL PFALVTAEGG QAMLEQARTR
GVAVLPKPLT LAMLDQWIAA QTLVD
//
