ID A0A372J6J7_9ACTN Unreviewed; 961 AA.
AC A0A372J6J7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Polysaccharide biosynthesis tyrosine autokinase {ECO:0000313|EMBL:RFU22797.1};
DE EC=2.7.10.2 {ECO:0000313|EMBL:RFU22797.1};
GN ORFNames=D0Z06_02670 {ECO:0000313|EMBL:RFU22797.1};
OS Geodermatophilus sp. LHW52908.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2303986 {ECO:0000313|EMBL:RFU22797.1, ECO:0000313|Proteomes:UP000262362};
RN [1] {ECO:0000313|EMBL:RFU22797.1, ECO:0000313|Proteomes:UP000262362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52908 {ECO:0000313|EMBL:RFU22797.1,
RC ECO:0000313|Proteomes:UP000262362};
RA Li L., Lin H.W.;
RT "Geodermatophilus marinus sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-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:RFU22797.1}.
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DR EMBL; QVQH01000002; RFU22797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372J6J7; -.
DR OrthoDB; 9812433at2; -.
DR Proteomes; UP000262362; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RFU22797.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000262362};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RFU22797.1};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..554
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 736..853
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT REGION 413..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 98740 MW; 6A2DA6385F1FDA00 CRC64;
MAGLSAATAD QLVRLGGAAA LGVLAVVLLR RSPQLGVGGW LAVVCLVPVW AGVGLGAYFE
PQVLAGLAAV GALVLVRRCV PLSPVGADLL IAAFALSALL PALVGRGTAN GVFVLLAHWA
SAYLLGRLAG HRLPLGRVYA LVAVAFTAVA VLALVEWVAG WNPFHLVPGS GGLREVWATI
QERGGVARAE GAFGHSIALG GSLALALPLT LAAPLRPAVR LGMAVLMGAA CAVTFSRIGL
GTAVLGVLLS IAFLRTGLPG RLRLLICGGL LVGAAAAAPL VTQVFAAAGD EASGSAGYRA
DLLSLLGEAR LLGLSPSYWR SPTGEASFGT FRSIDSALVL TTLTYGWIPL AFLGAAVLSA
VVVVVRGQAT APTVALVAQL PAFATVALIT QYASLVWFVA GLAVAAQALA PRGERAADPP
GPGDATARDP HRPHSLWGTQ PNPRRSMATV VAVGDRSGHR PGGDGIVGVA GYLQVLRRRM
WGVVVCVALA GGAALSASLL ATPTYTSTAG LFFSLQNGNT ASDLAQGATF TRAQMASYAT
LTTTPAVLDP VIDRLDLETT AGGLAGRVSA TAPNDTVLLQ VSASATSPTE AARIADAVAG
RLAEVVEEVA PADTEGRATV LVTPVAPAQV PTGPSSPDTT LNLLVGLVAG AALGVLYAML
RESLDTRVRD AVRVRALTDA PVLGLIAART QRAGEELVLA TDPRSAQAEL FRQLRTNLDF
LRLDGEPLSL AVTSSLPGEG KSTVALDLAL ALAEVHERVL LVDADMRRPA VAHRLDLEGS
AGLSTVLVGR AAVDDVVQEW GPHGLHVLTA GAVPPNPAQL LDSPRMTALM AELATRYDAV
VVDSPPVLPV TDALLLSRCT GGTLVVVDTH RVRRNQLAEA LRQLGNVDTR PLGVVLNRLV
REKQVYGYGA YGSDQGDDVD AGRWWRKGAR PAAVGRQHAV ETHDAVPAGQ RAPAAAGRPR
P
//
