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Database: UniProt
Entry: A0A0J1DG44_9BURK
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Original site: A0A0J1DG44_9BURK 
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
//
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