ID A0A494XME4_9BURK Unreviewed; 748 AA.
AC A0A494XME4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Polysaccharide biosynthesis tyrosine autokinase {ECO:0000313|EMBL:RKP50911.1};
DE EC=2.7.10.2 {ECO:0000313|EMBL:RKP50911.1};
GN ORFNames=D7S89_07550 {ECO:0000313|EMBL:RKP50911.1};
OS Trinickia fusca.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP50911.1, ECO:0000313|Proteomes:UP000280434};
RN [1] {ECO:0000313|EMBL:RKP50911.1, ECO:0000313|Proteomes:UP000280434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP50911.1,
RC ECO:0000313|Proteomes:UP000280434};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL Submitted (OCT-2018) 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:RKP50911.1}.
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DR EMBL; RBZV01000002; RKP50911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XME4; -.
DR OrthoDB; 9808257at2; -.
DR Proteomes; UP000280434; 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:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05387; BY-kinase; 1.
DR Gene3D; 1.10.287.1490; -; 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:RKP50911.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000280434};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RKP50911.1};
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 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..116
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 398..479
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 566..678
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 300..364
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 748 AA; 80941 MW; A50214B7C59CFFC6 CRC64;
MGMNFDNRYT DVSATDELRL TDYLQAIVAN WRLIVSITLA GLLIATGYAF LARPVYKADA
MIQVEDAQNA DNGGGGGNQQ QTIEPLSRMF ERKATTAAQV ELLRSRLVTE ATVNNLHIDI
TAQPRTLPVI GGLLAALTTG KWGFTVEPFM DLGGFAWGNE KMAMARFETP SSLYGKNFTL
TAGPAGTFTL ADPDGIAIAS GRVGEDVTGV SSAGPVLVHV DQLRARPGTQ FELSRASTVD
TVSHLQKALK VTETALQSGV IALSLEGSNP KLTADIVNGV ARQFIKQDMD RRSAEAEHTL
AFLDQQLPQL RHELDDAEQR YNTFRNSHGT VDLSEESRLL LQQVVDNKTK LADLQRQRAD
LSQRFTASHP AVAALDAQIA QLQSAQGQMS KSVAALPDTE QTALRLLRDV RVDTELYTNL
LNSAQQLRVI KAGQIGNVRV VDFAETPDEP VWPKRIIVIL IGFGGGLFVG IVVAFMKKAL
YGGVERADEI ENAIGVPVFA VVPRSGLQLR LQQNVMMRRQ GLHVLAAQSP QDIAVEGVRS
LRTTLQLSLD QAPNNIVMLT GSRPDAGKSF LSVNLAALVA SAGKRVLVVD GDMRRGEVHS
HFGVRHQPGL SDVLRGVEPH SVIQHEVLPG LDVLTKGTLP SHPSELLMSE RFHEVLESIS
RGYDLVIIDT PPVLAVTDST VIGKYAGTTL LVVRYGRHPI GEITETAKRL ETGGVNLKGV
LLTDVPPAMP ILGGSYNGGY YGYESISE
//