ID A0A0J7XU09_9SPHN Unreviewed; 508 AA.
AC A0A0J7XU09;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=V473_14775 {ECO:0000313|EMBL:KMS54508.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS54508.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS54508.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS54508.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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 -!- 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:KMS54508.1}.
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DR EMBL; JACT01000003; KMS54508.1; -; Genomic_DNA.
DR RefSeq; WP_066605767.1; NZ_KQ130435.1.
DR AlphaFoldDB; A0A0J7XU09; -.
DR STRING; 1420583.V473_14775; -.
DR PATRIC; fig|1420583.3.peg.2748; -.
DR Proteomes; UP000052232; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 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 InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF07536; HWE_HK; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KMS54508.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000052232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 252..304
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
SQ SEQUENCE 508 AA; 56287 MW; 49E34EC1779DD09F CRC64;
MAEERGLATD RATLLSLYDL DAGGFRNLDE ITGFAAQLCG VPIALVSIVE DVRQRFLSRV
GIDAEETPRD VSFCALAMLG ADIFLVPDAT RDPRFADNGL VTGPPYVRFY AGAPLVGADG
EALGALCVID TVPRADLTPL QRQGLTLLAR QVMVELEGRR RDRDMILRQR MDAAAVAESD
RMFRTLSDAM PQMVWSTLPD GYHDYYNARW YDYTGVPTGS TDGAAWNGMF HPDDQDRAWA
RWRHSLATGE PYEIEYRLRH HSGDYRWTLG RALPIRDGDG MIIRWIGTCT EIHEQKLMME
EREMIAHELS HRIKNIFSVI AGLIGLSARQ HPEIANVADD LRDRILALGR AHDFVRPHSA
ESAPQAGGGR GSLWGILDQI FAPYRGAAGP RIALSGDDPA IDDRSATPLA LLFHELATNT
AKYGALSVAN GMVHLHVSVE RGDVRIDWRE EGGPPVVPGR LDGFGSRLMT LSVERQLGGR
IERDWRPDGL RLSLWIPSRS MSRAAETA
//
