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Database: UniProt
Entry: A0A411WFT2_9GAMM
LinkDB: A0A411WFT2_9GAMM
Original site: A0A411WFT2_9GAMM 
ID   A0A411WFT2_9GAMM        Unreviewed;       718 AA.
AC   A0A411WFT2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Polysaccharide biosynthesis tyrosine autokinase {ECO:0000313|EMBL:QBH95171.1};
DE            EC=2.7.10.2 {ECO:0000313|EMBL:QBH95171.1};
GN   ORFNames=EKN56_01350 {ECO:0000313|EMBL:QBH95171.1};
OS   Limnobaculum zhutongyuii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Limnobaculum.
OX   NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH95171.1, ECO:0000313|Proteomes:UP000293154};
RN   [1] {ECO:0000313|EMBL:QBH95171.1, ECO:0000313|Proteomes:UP000293154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF-458 {ECO:0000313|EMBL:QBH95171.1,
RC   ECO:0000313|Proteomes:UP000293154};
RA   Ge Y.;
RT   "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL   Submitted (MAR-2019) 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}.
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DR   EMBL; CP034752; QBH95171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WFT2; -.
DR   KEGG; prag:EKN56_01350; -.
DR   OrthoDB; 9775724at2; -.
DR   Proteomes; UP000293154; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:QBH95171.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QBH95171.1};
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        32..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        426..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..108
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          367..447
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          525..648
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          255..289
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   718 AA;  80610 MW;  C870D6601E379398 CRC64;
     MSEIRSASYK NSKEEDEINL GKILGTIIDK KWLLVSITII LTLIGAFYAL FTTPIYRADV
     LIQIEKNSTN NLLNNVSEIL SNNIMPSTAA EIELIKSRMV IGKTVSDLGL NIEVSEKYFP
     IIGEKLSNLL GIKPGQVAIS KFDIPETMYN YDFILTVLPD NQYSLKGNDI DIIGKIALIE
     KSNNISILIS DIIAPVGTIF KIKKKDYLTT INNVLSDLSI QDTTKDGGIL RLYVTGQDKD
     KIRKIADSIS NNYLQQNVER KSEEAANSLA FLREQLPLIK RQLEEAEIKL NTFRQTNESV
     DLTLEAKSIL DSMVSITSQL NEVTFKEAEI SKLYTKEHPA YRSLLEKKNT LIQEKERLNK
     SVTNMPKTQQ EILRLTRDVQ SGQEIYMLLL NKQQELSINK ASTVGNARII DKAITQPNKI
     KPKSSLIILL SFIAGVFLSI LIIFIQELFR RTINDSSQLE SIGINVYANI PLSKNLKNRN
     RRLIKQPLEN HTKLLALEQE TDLAVEAIRS LRTSLHFAML DASNRILMIT GATSGIGKSF
     ISSNLAVVVA QSGVRVLLID ADMRKGGLHK LFKITMGNGL SDILSNNKEI EKCVYKTPVD
     GLDFIPRGSI PPNPSELLMN KYFSSFIEWA GANYDLIIFD TPPILATTDS MIIGRYSGTN
     LLVARFEHSS VREVEMSLKR FEQNGLTIKG LVLNAVQQRA SKFYGDGVFE YYSYQSEK
//
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