ID K8GR60_9CYAN Unreviewed; 788 AA.
AC K8GR60;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Capsular exopolysaccharide biosynthesis protein {ECO:0000313|EMBL:EKQ70209.1};
GN ORFNames=OsccyDRAFT_0484 {ECO:0000313|EMBL:EKQ70209.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ70209.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ70209.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ70209.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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:EKQ70209.1}.
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DR EMBL; AJUB01000005; EKQ70209.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GR60; -.
DR STRING; 864702.OsccyDRAFT_0484; -.
DR PATRIC; fig|864702.5.peg.518; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_2_2_3; -.
DR OrthoDB; 580971at2; -.
DR Proteomes; UP000001332; Chromosome.
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:UP000001332};
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..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..135
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 572..724
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 212..272
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 388..432
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 788 AA; 86487 MW; 1271F72FDBF607EE CRC64;
MQAGQNLQGL PLNGYNHLDS SSFASGDPGT EAAEGKPKGG FKLRPLLAIL WRNAFLIGGI
TAVAGGLGCW SYLKTPRVYE GNFTILVEPI TSQGRATDPT AISRAQVTQD NSSIDYPTLL
EVLQSPELLS KIAAQIQTRY PEVSSSTLAR DLNNQNFTVI RKGTNLLDST RTIDVTYRGT
DPQAVQFILD KLAEGYLRFS LEDRKTRIGG GVEFIEDQLP ALQQRVNNLE SQIQAIRQRY
RFNDPNLENQ EVADQLREVQ EKRLDAETLL REQTTLYGNL QNQLRLTPEQ GLAASALSQN
PRYQDLLAQL KRVESQIAVS LARFNEESPI VQRLREQERN LNRLILKETN QILGQSSPGV
PGSSQVVSFQ DALRVSLIGQ LVTSSNQAKA LQARISQIVA KENELNRRLT ELPALTRQYN
TLQQQLDIAT KTLNQFLLQR ETLRVEAAQK EVPWEIISKP KLATNILTGA PIARRSKKAL
QMVIAGFGAG LMLGVLAALL RERVRNVFVT ANDLQDAVSL PFLGVIPSAS NRVSGYSNGK
GIRVADPFIG AFSSLYANLR FLNPSSSIRS LAIGSVEPGD GKTTVALNLA QMAASMGQRV
LLVDANFYAP QIHTLLDLSN QRGLTDILRQ KVDLEDVLQR SSLDGNLSVL VAGPVQPDAT
KLFASNEMRS LAGQIQEMFD LVIYDTPALD GLTDVNFLTA QTDGMVMVVG VNKTKRSKFN
QILEGLKKYR LPVAGIVANH TVRGQAYYPI SPQESLPDGM PSAFLGKLKE PSDAAVRSAS
IVENFQDG
//
