ID A0A0Q5RG60_9SPHN Unreviewed; 745 AA.
AC A0A0Q5RG60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Capsular biosynthesis protein {ECO:0000313|EMBL:KQS04358.1};
GN ORFNames=ASG11_08920 {ECO:0000313|EMBL:KQS04358.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS04358.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS04358.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04358.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS04358.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04358.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQS04358.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMPM01000001; KQS04358.1; -; Genomic_DNA.
DR RefSeq; WP_055777938.1; NZ_LMPM01000001.1.
DR AlphaFoldDB; A0A0Q5RG60; -.
DR STRING; 1736350.ASG11_08920; -.
DR OrthoDB; 230260at2; -.
DR Proteomes; UP000051080; 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: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:UP000051080};
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 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..137
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 399..469
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 547..657
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 217..244
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 745 AA; 79760 MW; C0CFA6BBDF60B5C4 CRC64;
MASSGPAAPT NLTVTREQSR DVAVPFAGAG YGGYGTAKSS RELSLALLWR VLVEWRWLIL
AAIGIGLAGA VLVTLLTPLK YRSVATIELT PPEIEVISGE GSKGGRQTSA MRDVNFIGTQ
LGLLNSQALA ERVAQDLNLA SNPKVVGKGT DRTQNTKIAA SVVQSGTKVK LRPQSQLVDI
SFTARDPQLA SVIVNGITDA YVSTNLERRY ASSSYAREFL QRQIVNTRRE LEKSERQLTA
YAQQEGLITT GSSDTGGDTN SLTGSTLVAL NNALGATQAK RIAAEQRYRE AVLGGATTEG
SANAAPLRAQ IAALDAEYQQ KLQTFRPEYP EMVALRARID ALRASVTSET RTANSDRVGS
LRQEYQAAQG EENRLRAQVA GLSSSVLDQR GRRIQYTILQ RDVDTNRSLY DALLQRYKEI
GVASGIGTAV ASVVDRGPVP SGAFSPNLYL NLAIGAGLGF ILGMLAAIAL EFINDTIKTP
DDVRDKMQLP FLGGIPNAKL AKPIDELKDP LSPVTEAYLS TATALQFVAE GGAPKTLLMT
STRPAEGKST SAWALAQSFT RLGKTVLLID ADMRRPAFVT GKDEVGLSHV LTNGSSLSEH
VLQTEVEGLW IMPAGTVPPS PPELIASARF ASLLADAAAT FDHVVIDGPP ILGLADSPLL
STMVQATLMV VESGRTRTRA VVEAQNRLRT AGAHVIGAIL TRYQAQASYG YGYGYGYGQN
KDQYRYVADS NDKKRRIMLT TKNGD
//
