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Database: UniProt
Entry: A3WG58_9SPHN
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Original site: A3WG58_9SPHN 
ID   A3WG58_9SPHN            Unreviewed;       752 AA.
AC   A3WG58;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Exopolysaccharide biosynthesis protein {ECO:0000313|EMBL:EAQ28455.1};
GN   ORFNames=NAP1_12688 {ECO:0000313|EMBL:EAQ28455.1};
OS   Erythrobacter sp. NAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ28455.1, ECO:0000313|Proteomes:UP000002995};
RN   [1] {ECO:0000313|EMBL:EAQ28455.1, ECO:0000313|Proteomes:UP000002995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28455.1,
RC   ECO:0000313|Proteomes:UP000002995};
RX   PubMed=21952547; DOI=10.1128/JB.05845-11;
RA   Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA   Falkowski P.G.;
RT   "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT   sp. Strain NAP1.";
RL   J. Bacteriol. 193:5881-5882(2011).
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:EAQ28455.1}.
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DR   EMBL; AAMW01000002; EAQ28455.1; -; Genomic_DNA.
DR   RefSeq; WP_007165661.1; NZ_CH672390.1.
DR   AlphaFoldDB; A3WG58; -.
DR   STRING; 237727.NAP1_12688; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_2_1_5; -.
DR   Proteomes; UP000002995; 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:UP000002995};
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        49..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..126
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          419..487
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          566..708
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          239..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          327..375
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   752 AA;  81070 MW;  AF3842C43B89342C CRC64;
     MTDSTNLVPM RPLAAPAALL PPDLSASGER GGMRPVLVEY LDVLRRRKWV ILAVTLAAVM
     AALVITLLTR PTYTATTQVQ VSREQANVTN VQGVESENAG RDLEFYQTQY ELLEARSLAE
     RVVRSLKLDR NEDFWNAHGV DPAAIDKSSL AQPDQVNARA RAASAPLTDA RRSVSARERI
     AIETLLKNVS VNPIRGSSLI DLDYSSYDPE MSARIANVWV DEFIAQSIAR KFDSTAEARN
     FLEGRLDELR AKVEQSERAL VDFATQQGII TLTSDSGGQG TAQIREHTLA SENLQGLNAQ
     LIAATGERVE AQALARNSGS AQTNTTLARL REQRAVSAAE LAELMVQFEP GYPRALALEN
     QIAELDSAIS GEEARISRAA DEAFLAAQRR EAELRSRVAG LSGQVLSQRR DAIQYNIFQR
     EADTNRQLYD SLLQRYKEIG VAAVSASNIA VIDTAQPPQR PSSPNLLLNM ALALVAGTIG
     AGGLVFLLEQ STEGLSDPSK VHEALGIPLL GSVPQVPDHE DPVELVADPK TEIAESYIAI
     RSSLAFTTTQ GVPKSFMLVS SQPAEGKSLS ALALALVLGR MGKRVLLIDA DLRNPSAHAY
     LGTHRKVGLS NYLAGNDQVG ALIQNVRPNI DLMASGPSVP SAAELFSSDR LRELTARMAK
     EYDHVIVDSA PVIGLADAPL VSQAVEAVIF VAEAGRVSVR GLTSALERMA AAGSPIVGAI
     LTKLDQRSSH YGYGYSYSYS YSDRLEDERG AA
//
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