ID L8LZZ2_9CYAN Unreviewed; 778 AA.
AC L8LZZ2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Capsular exopolysaccharide biosynthesis protein {ECO:0000313|EMBL:ELS00675.1};
GN ORFNames=Xen7305DRAFT_00003760 {ECO:0000313|EMBL:ELS00675.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS00675.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS00675.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS00675.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS00675.1}.
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DR EMBL; ALVZ01000231; ELS00675.1; -; Genomic_DNA.
DR AlphaFoldDB; L8LZZ2; -.
DR STRING; 102125.Xen7305DRAFT_00003760; -.
DR PATRIC; fig|102125.3.peg.5139; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR OrthoDB; 580971at2; -.
DR Proteomes; UP000011203; 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:UP000011203};
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 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..130
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 598..725
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 201..235
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 778 AA; 87320 MW; 7B33D4ED0C8C122D CRC64;
MPENSLERTI SLSPQNGNGT YLYSMPMIEQ NAVLEEDDEG IDLRQLIRVI KHRLRLITLV
TIGVTSASIL WTVFQEPKYE GSFQLLVEPV TQGKEEDLLA ILGQNQEGMD YKTQIEVLQS
PIVLNPILEK LAVRYPEIEY EDLIKFRKSP LQIIRVDETK IIEVSYLDGD REKIEFVLDT
LAQDYLRYSL EERRAEVNQG IEFVENLLPD IRANVDQLQD KLQKFRQRYN LIDIETQANI
LSQQQLQIEE QFFAAQLELN ETRSLYENLQ QQLGKEPDEA IANSYLSEST RYQGLLDELQ
KIEISLAQES ARFSPQNPVI ITLEEKKAQL LPLLEKEAFR VLGKNYSEDQ DYITSAPSLS
SLRSKLDLEY IKAANQQELL KIRESSLATA LAELKTSIEQ MPVIAREYSD LELELTVATE
SLTRFLQAQQ ELQLEAGRQA LPWQMIASPK LEEDRVSPNP PLNIALGIMG GLLLGVGAAL
LAEKLDPVFH STEEIKEAIP IPLLGIIPTQ KDLKPLAEVA ENPETLSLPT LQIGGHVIDI
KNSPIPTSIV DQKNHQHQRY NASPFLEAFR SLNTNIKLLG SDANINSIVV SSSIPSEGKS
TVSSHLAQAA SAMGQKVLLI DADLRRPQVH LWTGLENKSG LSNILATGLP VEAAIKQVPH
WENLSVITAG DIPPDPTRLL SSVKMQKLME RLKCDRNYDL IIYDTPPILG FADGRILASS
TNGVVLVVRM GKTDRSLLKQ NLDNLKVSNV PVLGLVANRA NHNSNGSSYY SRYYSERK
//
