ID A0A401UAP7_9BACT Unreviewed; 771 AA.
AC A0A401UAP7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Capsular exopolysaccharide family protein {ECO:0000313|EMBL:GCC51988.1};
GN ORFNames=SanaruYs_22200 {ECO:0000313|EMBL:GCC51988.1};
OS Chryseotalea sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Chryseotalea.
OX NCBI_TaxID=2482724 {ECO:0000313|EMBL:GCC51988.1, ECO:0000313|Proteomes:UP000288227};
RN [1] {ECO:0000313|EMBL:GCC51988.1, ECO:0000313|Proteomes:UP000288227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ys {ECO:0000313|EMBL:GCC51988.1,
RC ECO:0000313|Proteomes:UP000288227};
RA Maejima Y., Iino T., Muraguchi Y., Fukuda K., Ohkuma M., Moriuchi R.,
RA Dohra H., Kimbara K., Shintani M.;
RT "Chryseotalea sanarue gen. nov., sp., nov., a member of the family
RT Cytophagaceae, isolated from a brackish lake in Hamamatsu Japan.";
RL Submitted (NOV-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:GCC51988.1}.
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; BHXQ01000004; GCC51988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401UAP7; -.
DR OrthoDB; 9794577at2; -.
DR Proteomes; UP000288227; 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; 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 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:UP000288227};
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 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..101
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 571..717
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 370..397
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 771 AA; 88595 MW; A2F6922C7EBC94FB CRC64;
MDKGFTNESE TIDFSKLKSI LLKNTVWILL LFILCNLSAY LYIRYTKNVY EAEAEIKLEV
NNEANEFGIT KIMEDQNLNL ISGEIELIQS NLFLSRVIDS LKLDVSYYSV GEFLDYELYK
NSPFKVTPIE VNNSYYNLNH TIDKKSEAQF EITLSDGEKL TGNFGKVVQM EGFKVLIESA
KGYTYEPKNT YSFMLNDAQA LRAYFTERLM VTPKNYNANT IRISFKEFSA EKAMDIVNKI
VNIYLGFSNE QKNFANKHKI DWVNNELEQI EEKMSQYEDY FKDFTLKNKT QDLTADMSRT
VEQINALDTS SFTINSRLRL IRKLKEDLKD GKTERYVSLT DKETLPQEVI NDVLAYQKKR
EAINELKLSY KESTFAYQEL QRDIEFAEKA LVIQLTELEK IVLDQARRAD TRRRLLEREF
ATMPDKATEY NKNQRYYKLY EEFYFTLMQS RSEFEIAQAG TIPDFKILSA ANLPGKPISP
KRILITIGGF TTSLVVIFFF VGFLYLIDDK ITSVHELERI AKVPILGIIP AFRNSRKDNL
PVQNQPHSMV SESIRTLRTN LDFFNVNGVQ KVISISSTVS GEGKSFVARN LGAVIAMSNK
RVVLVDLDMR KPKDDQPPPF NNKALGVSGV LIGKNTWQEC AQSTSVANFD VIPAGPHPPN
PSELLVNGAF EKLIQELRQA YDFVIIDTPP VGIVTDGIMA MKRSDVCVYL FRANYSKKEF
LHNLKRINSL HNFSNVTAIL NALPATAQTY GYGYYHEEKK SKYFESIFFN R
//
