ID D8FWI2_9CYAN Unreviewed; 774 AA.
AC D8FWI2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Capsular exopolysaccharide family protein {ECO:0000313|EMBL:CBN54722.1};
GN ORFNames=OSCI_1040007 {ECO:0000313|EMBL:CBN54722.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54722.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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; CACA01000101; CBN54722.1; -; Genomic_DNA.
DR RefSeq; WP_007353947.1; NZ_CACA01000101.1.
DR AlphaFoldDB; D8FWI2; -.
DR OrthoDB; 580971at2; -.
DR Proteomes; UP000004532; 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:UP000004532};
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 51..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..134
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 579..703
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 207..234
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 383..434
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 774 AA; 86486 MW; E1E8498ABB1FA150 CRC64;
METEQGDKIV SIGKRGRQFQ ELPVVDTDES SPQPQKGLNF APFLRTFRRK AWLILAITTL
VAVGAGFYIK TSKKTYQGDF RLLVEPVTNE ARIAEPSTLA RSDSAVPSRD IFSLDYPTQL
EILQSPQMLN AIVDRIKTKY PKFTYEEFQR GLLVIRVGSN LLDQTKIIEV RYLGQDPEMV
QFILDEMAKK YLKYSLEERK SRIGEGVKFI EDQLPGLQQR VNDLKSRLQQ LQQQQRISDP
KVQGEELLTQ VRTIETQELE TQRLLEEQRS LYANLQKQLD FTPNEAIAAS ALSEEPQYKE
LLVKVKEVES QIALESARFK SANPLLEALE RKRANLLDLL NQQTQRIIGQ NLGVDANNSK
VMRFQNSIRV GLIKQLVDTA NQIQVLEVRN QAISQARDDL NRQAKLFPAV ARQYNELSQQ
LEIATKTRDQ LLTQRETLRV QAAQNQVPWE LISKPRIPLD PAGNLEPAPS KAKNKFAMAV
VGALVLGMLA ALWIEKRRNI FYVAEDIKDA IQLPMLGVIP LDKDSEKLAR DYRNGYASLV
SNDLASRSSS PFLEAFDALY TNLCFLFSDR QIGSLTIASA APGDGKSTVA LHLAEVAALA
GQRVLLVDAN LHSPTLHTLL DLPNFRGLSD LLCNKLEPND IIQRSPLADN MFVLTAGIPL
PGAARRMSSS FMAHLMEEFQ TKFDLVIYDT PPLIDAKDAN FIGARTEGIL MVVAVLKTKN
SVVKQVLSQL ESFGIPCLGV VANHVGKNAK SKGEKAVVLK PSRQVGLSAP APQE
//
