ID B2JGR5_PARP8 Unreviewed; 730 AA.
AC B2JGR5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:ACC70250.1};
DE EC=2.7.10.2 {ECO:0000313|EMBL:ACC70250.1};
GN OrderedLocusNames=Bphy_1061 {ECO:0000313|EMBL:ACC70250.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC70250.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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}.
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DR EMBL; CP001043; ACC70250.1; -; Genomic_DNA.
DR RefSeq; WP_012400464.1; NZ_CADFGH010000007.1.
DR AlphaFoldDB; B2JGR5; -.
DR STRING; 391038.Bphy_1061; -.
DR KEGG; bph:Bphy_1061; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_0_0_4; -.
DR OrthoDB; 9808257at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
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 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACC70250.1};
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 23..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..103
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 381..460
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 545..661
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 326..374
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 730 AA; 78692 MW; 43FFEF382305E4B7 CRC64;
MQARTEEEDV VLGQLLQVII DDIGWLIGIA ATIVAMAGFY CYVAKPVYSA DAHVRVEASD
NTSQALTQTQ TGATISTGQN TIPTDAEIEM IKSRGVVAPV VQQMKLNFSV TPKTLPILGS
LAARVATPGQ PAKPWLGLGS YAWGGEVAAV DSIDVTPALE GQKLILTAMD NGRYTLMTPD
GQLLLRGQAG EPAQGGGVTL FVKQLVARPG TQFTVMRAND LDAIAAFQSA INVQEQGKQT
GVISISLEDQ SPEHAAAVAN ALAQSYLLEH IRTKQADASR MLDFLKSEEP RLKSDLEHAE
AALTAYQSKS GSINASDEAK VYLEGSVQYE QQISALRLQI SQLEQRYGDD HPMIKAAQQQ
MAELQAQRTK YADRFRDLPA TEVKAVQLQR DAKVAEDIYV LLLNRVQELS VQKAGTGGNV
HIVDAALRPG SPIKPKKVLI LSAATILGLI VGTGFVFLRR NMFKGIDDPE TVERAFHLPV
YGLVPLSAEQ ALLENAAVRG GARERAVLAN AKPKDVCIES LRSLRTSMQF TLQDARNRIV
MFTGPLPGVG KSFLTINLGV LLAHSGKRVL MIDGDMRRGA LEKHVGGSPD NGLSELLSGQ
ISLEEAVRAT EIDNLSFISC GRRPPNPSEL LMSPRLPQYL DGLAKRYDVI LIDTPPVLAV
TDASIIGGYA GSTFFVVRSG MHSEGEIADA LKRLHSAGVH VQGAIFNAMP PRARGNYDRS
YAAVQEYLST
//
