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Database: UniProt
Entry: A0A212TK58_9BACT
LinkDB: A0A212TK58_9BACT
Original site: A0A212TK58_9BACT 
ID   A0A212TK58_9BACT        Unreviewed;       797 AA.
AC   A0A212TK58;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:SNC66427.1};
GN   ORFNames=SAMN06265337_1607 {ECO:0000313|EMBL:SNC66427.1};
OS   Hymenobacter gelipurpurascens.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=89968 {ECO:0000313|EMBL:SNC66427.1, ECO:0000313|Proteomes:UP000198131};
RN   [1] {ECO:0000313|EMBL:SNC66427.1, ECO:0000313|Proteomes:UP000198131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11116 {ECO:0000313|EMBL:SNC66427.1,
RC   ECO:0000313|Proteomes:UP000198131};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FYEW01000001; SNC66427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212TK58; -.
DR   OrthoDB; 9794577at2; -.
DR   Proteomes; UP000198131; 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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..103
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          604..764
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   797 AA;  89060 MW;  87E47D06542A6D0E CRC64;
     MEQRPAPHAD EIDLHELFFR LRNRWQLFLL ALLLAGSAAF LYLRLKAPIY SFRSTMLLGN
     QSSGSKRAQE LLQILEVQDK GTKMEDEIGL LTSTDMVQRA MSRLPFNVSY FAASDTWLNT
     FGDLQVRERG MGTVPFRVTP VMSAPQLTGT RIYVDPLPGG KFRLHAEADK AWLVDLPSGE
     LMQEVLDVKF DRTVQAGDTL RSPMLTAVIQ AEPGYEDATS KERYYFQLYD QADLADEYQS
     RLTVRPVDRE SRIIELTSKG TVPQKEVQFL DTLMRVFVED ELRDKNTTGQ KTVAFLNKEI
     GQLSDSVRKS TAALSSFRAA RGMVDVTAQS SAGIQQQGEL QMTRAKIATN RKYYQNMLSY
     LRANQGATQI VSPSSVGIED PVVNNLILQL TDLNSQRAAL GVNASVDNPM VTILDERIRS
     AKQALAETLI NMTRATDIAL RDLDAQLAKV RGTMNQLPEN ERQLASLKSK TDFNDKNYQF
     LIEKRAEAAI ALATNSTDKK VIDEASMTGG GPTEPKPVLV GLIALLAGLG IPFGISMLMD
     KANRRIQSKE DLSRITTIPM LGVIAHGTKQ DKVTMFTDPK GPIAESFRSI RVNLQYLSAG
     LDKKVIGVTS SVPGEGKTFC AVNLAAEMAQ SGRKVLLLEC DLRRPTVASY FDLGPNCAEH
     GLSSYLMGLS TVEEARHATG VRSLDVMCCG PIPPNPTELL ESPRMTELME QLRTEYEYVI
     VDTPPVGYVA EFFMLLRHLD ANIYVVRQNY TDKGLVSHIN ELHQEKKIKQ IYMVINDVHF
     TKTYEYRYKE KAYTYGY
//
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