ID F4XQW4_9CYAN Unreviewed; 762 AA.
AC F4XQW4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Capsular exopolysaccharide family protein {ECO:0000313|EMBL:EGJ32939.1};
GN ORFNames=LYNGBM3L_56010 {ECO:0000313|EMBL:EGJ32939.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ32939.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL890874; EGJ32939.1; -; Genomic_DNA.
DR RefSeq; WP_008183210.1; NZ_MKZR01000001.1.
DR AlphaFoldDB; F4XQW4; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_2_2_3; -.
DR OrthoDB; 580971at2; -.
DR Proteomes; UP000003959; 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 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..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..132
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 576..691
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 405..432
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 762 AA; 84281 MW; 9C31F2C47AC91B94 CRC64;
MGSQGAYKPS LSNHSGQQQY RSSPQLTGGA YELEASKLDL RRILAAARRR AVLMAGVALT
VTSGIIAKTL SAVPIYEGKF QLLLEPSSGE DPLELQGKPG VNSIAAPTTS FDYDTQIQLL
SSPQVMSEIV EQIQTQYPEI NYHTLREGIM VSRLRETKIL EVAYQDSDPE RIQFVLEKVA
LGYIEYSKQQ QQASIRQGIQ FVSNQQPKIQ GQINQLQLQL QQLQQKYNLI NPQLQGQLLT
NRVNAIVEHR KATQTQLRET IILYGKLKGQ LGLSSQQAEA VAKLIETPRY QQLLSQLSNL
ESQMVLDLAQ FKENQSTFDG LRQQQQNLLP LLSQEAERVM TSRIQEFGGN PQSASSSTLR
LNLIQQLVET ANQIKVLEMR QAAITKGESL MSEQLKQLAV IANRYTELKQ KIEVATESLN
RFESVRETLE LESAKTSIPW QTIVEPQQPQ KPISPNLPDT LLLSAVAGIV AGATAGFLAE
KLHHLLNSTD DIKEYTRLPI LGTIPFNKEL QKSNTVTGVG IIPEPEASAP QLGVGSGSYQ
ISPVLEAFRS LQVNLQCLYS EKPISAIVVS SAEPADGKST TAIFLALAAA AMGQKVLLVD
ANLRFPQIHQ KMDLPNLWGL SDVLSSEIKV DDVIQRSPLE ENLCVLTAGQ ISTDPTRLLN
SPKMQNLVQY LKERFELVIF DTPPLLGLAD ARLLEPNTDG ILMVVGLGKA NQVLFKEALS
ELRIAHSTVL GIVANGLKGY TTRAYDYYHY YFGNTLEETK VS
//
