ID A0A0K8NZQ0_IDESA Unreviewed; 463 AA.
AC A0A0K8NZQ0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tyrosine-protein kinase wzc {ECO:0000313|EMBL:GAP35853.1};
DE EC=2.7.10.- {ECO:0000313|EMBL:GAP35853.1};
GN ORFNames=ISF6_1626 {ECO:0000313|EMBL:GAP35853.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP35853.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP35853.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:GAP35853.1}.
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DR EMBL; BBYR01000029; GAP35853.1; -; Genomic_DNA.
DR RefSeq; WP_054019885.1; NZ_BBYR01000029.1.
DR AlphaFoldDB; A0A0K8NZQ0; -.
DR STRING; 1547922.ISF6_1626; -.
DR OrthoDB; 9150572at2; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR Pfam; PF02706; Wzz; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GAP35853.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037660};
KW Transferase {ECO:0000313|EMBL:GAP35853.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..113
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT REGION 242..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 248..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50244 MW; 9B10707958152386 CRC64;
MTGPAPLFPV RPDAPDGEFT LRDLLRLVAK HGWVVLVCLL AGGLVGAGIY AIQKPVYASV
ARVWVKTEQG SPSFLSGVTA YREPLYPDPV NRRIETEMEL MLTRTSAAQV VRNLKVRPEQ
LPSTPLAQLI AASGLVAAKP ASDGAASNRL IDDFLKAVSV EPLRSKTADT TSNILEVRFE
ASDPALAPQA LSQLISNYLG VAATQNRQLG EEAARLLGAE VEQARGELMA LDAQIVALAS
RPPPRAAAEE GSGKRARSER GERGERSSER RSRRENTFAG APVGNEQALA ALKTQTVEMQ
AELDALRELY TDDAENVRTL RRRLEAMQRR LAEGLSASVQ AVSSLGSLER QRALAQDRYN
EVQKKLDQIK LYLRLNPSDA ESRVIVDAPS RPLDDEGKKR VVVALIGPVA GLLLGLLLAG
LRELSDQRLQ SRRDVRQALG LPVLGALPRL PAGERRRLAG EAR
//
