ID A0A090AJJ5_9GAMM Unreviewed; 738 AA.
AC A0A090AJJ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Capsular exopolysaccharide biosynthesis protein {ECO:0000313|EMBL:BAP55095.1};
GN ORFNames=THII_0798 {ECO:0000313|EMBL:BAP55095.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP55095.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP55095.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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; AP014633; BAP55095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AJJ5; -.
DR STRING; 40754.THII_0798; -.
DR KEGG; tig:THII_0798; -.
DR HOGENOM; CLU_009912_2_1_6; -.
DR OrthoDB; 9775724at2; -.
DR Proteomes; UP000031623; 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; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623};
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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..111
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 394..468
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 552..697
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 220..277
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 361..388
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 738 AA; 82760 MW; 693D9727EA71405B CRC64;
MEMPTLQPSQ LANLASGEDE IDLRVYWNVF NKHKWQIIGL TLLIGLLTTL VTFSLQPIYR
ATVTLLIEFD QPKIISIEEV YGVSSANKDY YQTQLEILKS RSLVEKVVDK LNLVSHKAFN
QDTSPVWFWD WRHWWVQLNE SAATPISAEE KYQAIVNMIA ANLGIEPVRN TQLAKISFES
KDAQLAADIA NTLANLYIET DLNARIALTK KATTLLTERI NDLRQKLSHS EQVLQAYLEE
HNLVNVEGVK SVAIKQIEEM ASNLVKAHQQ LAETQSAYNQ VQALRGQASG AFESITAVIN
NPLVQRLKEI ELDAEKKVSE LSKRYGSKHP NMIAATTELN TAQANTTKQI RQVITGITKE
YEVALANVQA LERSLKEKEN QIQDINRNEY QLAVLQREVE VNRQLYDLFL TRFKETDASQ
DIQALQSKIG QVIEPALVAS TPYKPQKKLI VAISLVLGFL FSTLLAYLLE YLDNTIKNGE
DVEQKLGLPL LGTLPKLKIS KQDPCHPQLM FLEKQTSQFA ESVRTIRTGI MLSNLDTPRK
VLVVTSSVVS EGKTTFAINQ ALALGQMEKT LLIDADMRRP SIASVFGLTD KAPGLSELVA
GTKQLAECIH PVMDGNIDCI HSGLIPPNPL ELLSSRRFKE LLTQLEKHYG YIVIDSAPTL
AVSDAIVLAT AASAIVYVVK ADVTPYQMVK EGLKRLYQVN APVLGIVLNQ INTRKLSHYY
SNKYGYYNKP GYYSYTNR
//
