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Database: UniProt
Entry: A0A1I6DVM4_9RHOB
LinkDB: A0A1I6DVM4_9RHOB
Original site: A0A1I6DVM4_9RHOB 
ID   A0A1I6DVM4_9RHOB        Unreviewed;       685 AA.
AC   A0A1I6DVM4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:SFR09539.1};
GN   ORFNames=SAMN04515673_105254 {ECO:0000313|EMBL:SFR09539.1};
OS   Poseidonocella sedimentorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Poseidonocella.
OX   NCBI_TaxID=871652 {ECO:0000313|EMBL:SFR09539.1, ECO:0000313|Proteomes:UP000199302};
RN   [1] {ECO:0000313|EMBL:SFR09539.1, ECO:0000313|Proteomes:UP000199302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC   {ECO:0000313|Proteomes:UP000199302};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOYI01000005; SFR09539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6DVM4; -.
DR   STRING; 871652.SAMN04515673_105254; -.
DR   OrthoDB; 230260at2; -.
DR   Proteomes; UP000199302; 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:UP000199302};
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        30..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        402..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..107
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          345..418
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          494..650
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          219..282
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          309..350
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   685 AA;  74357 MW;  3BBC2295ECBA0535 CRC64;
     MAKPSILGED ATQEIIDLGA LFARLWRGRF VLALAAMVGF GLGGVYAYLL AEPEYEATAS
     VVLETRSEKV VDLDSVIGGL SKDLPALNTE VEVLRSRRLL GQVVDALALT EDAEFNPTLA
     EPGLKARLKS RVMSLISDAE PVVAPQQDAQ REKAITRLQK RTSVANLPLS LVFQIKVASA
     EADRAVAIAD TIAQTYVDQQ ISVKYEATEQ AVAWLTDRVS DLKQSLKISE DRIKAFRARS
     DVIGPDSIDQ LDRQLKALRG RITDQELAIE AARARLTAAR EEARSAPPVT QPQPASTASL
     LRASTLRPVA RAEAEVQLAE TRLQALVSAA EELEETLARQ NTELQEFQQL TREADASKLL
     YEYFLGRLKE TSVQQGLQRP DSRILSNAVL PDGPARPQKA RILGLSLVLG LFAGIGLLAL
     SDLRQKGFRD VTALQDATGM TVFGQVPELP GATRSELLSR LASEPSSMAA EAIRNIRTSL
     LMSRLDDPPK VVMITSSVAD EGKTILSLAL AQNIAALGQK VLLIECDVKR PSFARVLRSE
     RKEGLLSVVS GRTELQNAVL SDGETGLDIL MCESANPASA DMFSSRQFQR FIEAARESYD
     HILLDTPPVL LVPDARVISR VADAILVALR WQSTSRRKLS DGLAALETVN ARAAGIVTTR
     VDPQALDYGA HLYELREPGP SSIVA
//
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