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Database: UniProt
Entry: A0A316FWC6_9RHOB
LinkDB: A0A316FWC6_9RHOB
Original site: A0A316FWC6_9RHOB 
ID   A0A316FWC6_9RHOB        Unreviewed;       758 AA.
AC   A0A316FWC6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Capsular exopolysaccharide synthesis family protein {ECO:0000313|EMBL:PWK53114.1};
GN   ORFNames=C8D95_11416 {ECO:0000313|EMBL:PWK53114.1};
OS   Silicimonas algicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1826607 {ECO:0000313|EMBL:PWK53114.1, ECO:0000313|Proteomes:UP000245390};
RN   [1] {ECO:0000313|EMBL:PWK53114.1, ECO:0000313|Proteomes:UP000245390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 103371 {ECO:0000313|EMBL:PWK53114.1,
RC   ECO:0000313|Proteomes:UP000245390};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-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:PWK53114.1}.
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DR   EMBL; QGGV01000014; PWK53114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316FWC6; -.
DR   KEGG; salo:EF888_06220; -.
DR   OrthoDB; 230260at2; -.
DR   Proteomes; UP000245390; 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:UP000245390};
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        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..114
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          414..485
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          568..697
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          235..269
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          352..432
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   758 AA;  83994 MW;  059EE11DA49200C8 CRC64;
     MRQESTLKFR TMRVGDAPVE DDSDDEIDLR AIISKLWRGR WIIIISTLFA GLIGFFLTSQ
     YEATYTARTK VMFDIDQANV VDVGQSVVRI DDTLENQVEI LQSTTLIERV IGELNLLENP
     AFNSSLRPPR ETLGTRIRGI FSMPDGVKEV LRDVGLMSPP PAPPDAAEAA ALLRLQIISQ
     IRNSLKLSPI WDTKVIEIGY TAGDRNLAAR VANTFAQQYI TDQLEAKLEA TREATTWLSN
     RVEELRQRVQ DAEEAVEAAR AELAADAGQS LEITQAQIEA QNAGLSIARN DLSLAQATYG
     RLRDAVDAGR DFGAINEFRA SPLIQTYRAS EDTLMSQQTA LGDTVDEDHP ARVRLAQQLS
     DVRENLQREA ERIVEGARIE VAVQTDRVAS LEAELDELEI LARGQSQDTI RIRQLEREAE
     ASRAVYENFL GRLKETTEQE ALQTADARIL SPAEVPLGPD AARARRTQLL SLILGAMAGV
     GLIFLIDLLN NTFRAPDQLE QLTGLPYLGA LPSAGRRLHR RDVVTQFRTS PKSALAEAVR
     SLRTSILFSK VDEPPRTVMF TSSVPREGKS TTSMLVAMTS RQMGKSAVII DCDLRLPSLA
     RLLPDEGREQ GLLSVLDGTA TMDDAIYHDE ETGLDVLMTV PSEPRSNINA ADILSSRKFH
     EIVAELKARY DLVIFDTPPS LVVADAKILS RLVDAVVYVV RWDSTPRGAV QEGIKELQSV
     GAPLIGVSFT MLNEARAARY SYDGYSYYRG RYKDYYVS
//
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