ID A0A0J1DG44_9BURK Unreviewed; 761 AA.
AC A0A0J1DG44;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Tyrosine protein kinase {ECO:0000313|EMBL:KLU38033.1};
GN ORFNames=AB595_02940 {ECO:0000313|EMBL:KLU38033.1};
OS Massilia sp. WF1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU38033.1, ECO:0000313|Proteomes:UP000036336};
RN [1] {ECO:0000313|Proteomes:UP000036336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA Lou J., Gu H., Wang H., Xu J.;
RT "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT contaminated soil.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001074};
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 etk/wzc family.
CC {ECO:0000256|ARBA:ARBA00008883}.
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:KLU38033.1}.
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DR EMBL; LELH02000003; KLU38033.1; -; Genomic_DNA.
DR RefSeq; WP_047822232.1; NZ_LELH02000003.1.
DR AlphaFoldDB; A0A0J1DG44; -.
DR PATRIC; fig|1406431.3.peg.3406; -.
DR Proteomes; UP000036336; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05387; BY-kinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR005700; EPS_ExoP-like.
DR InterPro; IPR032807; GNVR.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005702; Wzc-like_C.
DR NCBIfam; TIGR01007; eps_fam; 1.
DR NCBIfam; TIGR01005; eps_transp_fam; 1.
DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR Pfam; PF13807; GNVR; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KLU38033.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000036336};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..129
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 411..490
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 571..689
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 297..338
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 761 AA; 83739 MW; 73870808A2911AC3 CRC64;
MNIHGEPNSL SRVVHPSPIA GIPFDARTVE GSPDEPAFDL KGYFHTLYDN RWLIGGITAF
ITLVAVLYAL VAKPVYESNL MIHVEEESPN ASKNILSEAS SLFETKKAAI AEMELLRSRM
VVSRAVDNLQ LYIDVQPKYF PIAGFWFANQ NNNGLSDPGL FGYGGYVWGA EKAEVSVFEV
PESWLGREFN LTALGNGRYR FSGGGQRIVF DGAVGLGYRV PTPEGMVELK VDRMAANPGA
RFRLRRISRV AMIQAIQSAL VITEQGKQSG IIEVKLQGEN ARRTHTLLSE IGREYMRQNL
ARKTEEAEKS LAFLNQQLPI LKRQLEQAED RYNQFRNANG TVDLQEEARM SLAQAAAARA
RRIDLIQKKT ELLSRFTEDH PVVAAINRQR KEVDAEIEEV NARIKALPVL EQDEARLTRD
IKVNTDLYTA LSNTAQQLRL ISVGRVSNVR MVDAPVPPEK PIKPNRPLIV ALAVVTGLFL
GTLVAFARKA MKGGIDDPQR IERLLRARVV YATIPHSSNQ DKLTRKTRDD AEPLPLLANI
IPEDAAVESL RSFRAALQFS MPHFKNNVVM FAGPTHGLGK SFVSANFAAV MAAAGKRVLL
IDADFRSGRL HRYFGVNPDQ GLSKAISGAA SATEIIHHNV VENLDFIPTG PLPPNRSEFL
LDVNLSALLD TLSADYDLVL IDTPPILAAA DALIIGAQAG AVFLLARASV TTEAEITESI
KRLNYAGMSP QGVLFNDMTY GIARYSTLHQ ASPANQLAFT G
//