ID A0A2N0FWF9_9FLAO Unreviewed; 842 AA.
AC A0A2N0FWF9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Capsular exopolysaccharide synthesis family protein {ECO:0000313|EMBL:PKA98785.1};
GN ORFNames=B0O79_2478 {ECO:0000313|EMBL:PKA98785.1};
OS Flavobacteriaceae bacterium MAR_2009_75.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250285 {ECO:0000313|EMBL:PKA98785.1, ECO:0000313|Proteomes:UP000232536};
RN [1] {ECO:0000313|EMBL:PKA98785.1, ECO:0000313|Proteomes:UP000232536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_75 {ECO:0000313|EMBL:PKA98785.1,
RC ECO:0000313|Proteomes:UP000232536};
RA Teeling H.;
RT "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT Genomic & Taxonomic Observatory).";
RL Submitted (NOV-2017) 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:PKA98785.1}.
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DR EMBL; PHTZ01000001; PKA98785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0FWF9; -.
DR Proteomes; UP000232536; 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:0009103; P:lipopolysaccharide 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 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 24..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..106
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 462..529
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 602..726
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 842 AA; 95071 MW; 09C1D8A507109EFE CRC64;
MTNQIFVEEK PIDVTELIGA YLRYWQWFVL SALVALILSV IYLKLTKPVY RSQASIIIED
EKGKPNSSAA GGFVDLGMIE GLSTSSIENE IGLISSRRLM TNAVKALGLQ MVHYTSGDII
GIKSEKLPIK ELYKQTPYKL RLVRTDKSKL RQAIEYEQNI LEITMLSDEK VRIEQLEGNY
KATHSFGDVV KLNFAEFIVE KNNTVLQQED EDEDEEELRI FRVKFLSYEA VANTLRKQLE
VSLVDDNSTL IQLAINNRVA EKAEDILDQL VFEYNQEAIE DKNLIARNTA FFIDERLKII
NSELDSVESG KEEFKTSNQL TDIQTESSII IQNVSDYNNK QQEIATQLEV TNAMMEHVSN
DQLSLLPTNM GVGESSLGLF VDEYNQLVLE RNRLLKGATE TNPLVVNMTN QLREIKENIR
QSLISTRSNL RITRDNIRRQ AGILGSQISE KPSQEREYRG IERQQNIKES LYLFLLQKRE
ENSLSLAAKA PKAKIVDEAY RLEAPVSPNT KMVLGLGLIG GLLIPFLVIS GKRILDDKIN
TRDDIKEYTE AIPILGEVPH ISSDGPTLVS GDERSILSES YNILSANLNY ILTKEEPSTK
GKCIYITSSA QGEGKTFTTI NMAMTLAETG KKVIIVGADL RNPQLHRHEK NGLAKEGLST
YLTDDRKSIL EYVEASSLHT GLSVIPSGPI PHNPIQLLRS EKIAPMLEQL KEVFDYVIVD
TAPAMILADT FLISRYADLT LYLIRAGKSK KRVLEFALES YAEGKFINPI FLLNDVNMAD
ASYGYKYGYN YGKEQEVSPI DYILKKTKSI FSKSNLEKIK SLFSKSNLDK LKSLFTKSKK
KK
//