ID A0A2P1PU67_9GAMM Unreviewed; 773 AA.
AC A0A2P1PU67;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Capsular biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C7S18_14855 {ECO:0000313|EMBL:AVP98387.1};
OS Ahniella affigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Ahniella.
OX NCBI_TaxID=2021234 {ECO:0000313|EMBL:AVP98387.1, ECO:0000313|Proteomes:UP000241074};
RN [1] {ECO:0000313|EMBL:AVP98387.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP98387.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Ko Y., Kim J.-H.;
RT "Ahniella affigens gen. nov., sp. nov., a gammaproteobacterium isolated
RT from sandy soil near a stream.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AVP98387.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP98387.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Keele B.F.;
RL Submitted (MAR-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}.
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DR EMBL; CP027860; AVP98387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1PU67; -.
DR KEGG; xba:C7S18_14855; -.
DR OrthoDB; 9775724at2; -.
DR Proteomes; UP000241074; Chromosome.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000241074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 53..144
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 417..493
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 577..687
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 297..352
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 773 AA; 85780 MW; 3171A0B8E7396D5C CRC64;
MGLKVQDGLV RALINSPAAN IHLFRGQRNF AMNSVSRPEE LELEGPEQRE LPNLQDYLRI
LFRYKWGILV LMIVGGVISA LRAMSEVPLY DATATMLIER QAARFVSIEE VYRGSQGWDF
GEYYQTQYEI LRSRPIAERV VDKLGVEAFN KRQGNAKPAF SWRNLFGGAP EPAPAAAPVD
PKIAREVAIN TVIGSLDVMP VRNSQLVRIR MRGPNPEFAA MLANTHAQAY IEEMLEGRLQ
MTQTASQWLN ERTKGLREKL EASEKTLQEF RDRERLLDVK GVDSLASTEL GLASERLAEA
RRERIDKETA YNQIRNARSL EEVPALLVSP IVQEYKTALT QAESEVRELS QRYGARHPKM
AEANTKREAA QASLGRQLKI AANAVEGEYR AAVSRENALS GELGAAKGEL LDLNRKQYEL
TALEREVDGN RQIYELFQNR FKETSASGGV QTANARLVEN AQIPNAQVWP NKRRATMIGL
LIGLALGMAL ALILDHMDNT LKGAEDVEKR LGLAVIGLVP KLKSLSEGGE LPINYFGAHP
QSSFSEAIRT IRTGVLLSAV DETHKRILIT SSVPSEGKTT LSMNLATALG HMKKVLLIDA
DMRRPSIHKG LPDQRQSPGL SEYITGERKI SECMRQIEGS NLFVMPAGVA PPNPLEILSS
RKFAESLEAL SRAFDHVIID CAPACAVSDA LVLSKLVHGV VYVVRSDSTQ WQIARSGVKR
LRRIDAPLIG AVVNQVVPRR TGYAYGKYYY HGDGYYSDYG YAKSKSRSKN KGS
//
