ID E4T1G6_PALPW Unreviewed; 797 AA.
AC E4T1G6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:ADQ78560.1};
GN OrderedLocusNames=Palpr_0399 {ECO:0000313|EMBL:ADQ78560.1};
OS Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ78560.1, ECO:0000313|Proteomes:UP000008718};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB4;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ78560.1, ECO:0000313|Proteomes:UP000008718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17365 / JCM 13257 / WB4
RC {ECO:0000313|Proteomes:UP000008718};
RX PubMed=21475585; DOI=10.4056/sigs.1503846;
RA Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Paludibacter propionicigenes type strain
RT (WB4).";
RL Stand. Genomic Sci. 4:36-44(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}.
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DR EMBL; CP002345; ADQ78560.1; -; Genomic_DNA.
DR RefSeq; WP_013443929.1; NC_014734.1.
DR AlphaFoldDB; E4T1G6; -.
DR STRING; 694427.Palpr_0399; -.
DR GeneID; 78490011; -.
DR KEGG; ppn:Palpr_0399; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_6_0_10; -.
DR OrthoDB; 9794577at2; -.
DR Proteomes; UP000008718; 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 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:UP000008718};
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 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..115
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 585..706
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 797 AA; 90146 MW; 70ECB03903F142C4 CRC64;
MDNNFEQFEQ DIQEKPIDWR EIFERIIFHW KWFLFSAVIA IIAGFFYSRT QNDVYEVKSS
ILIIDQSKSG QMNELSVLKQ LDAVGIGGGK SATMANNEEQ VIHSTTLMKR VVNNLELHTN
YSHKVFLKSE DLYTASPLYV HLDSLSLNQL QFPLELDITP EDGQLNIKGN YNDSTFQLQA
KKLPAILKTP AGIISILLRH GKTFPDEPIK VSISNPSKVA KYLAEKSLTT EVGKLADVID
LTLKVAHAKK GQDILNTLST IYNQDATEQN NLSAINTATF IDGRLKLLAS ELGDVEKDVE
SYKKTNKLTD IDEDAKMYLE KNSTYNQLQV QVEMQQHLIK YVDEFINNPA HQSALIPNLG
LTDVGLVAVI QKYNELLMTR GRIALGSSSE NPVLKTLNEQ INATRKAIQI SISNIRKGLQ
ISNTDLGAQN SLIQSKIRDM PRQEREFIEI KRQQQVKESL YLFLLQKREE ASLNMAVTVP
KGRVLNAPDD ATQVGPHRTM IMLMFLVIGL LIPAAIIYLL EIINTSIRNR TDVEKSTKIP
VISELGHNDS SSIFIDYHTN SSSNSELFRL LRAKLQFTLD HPTEKVILVT STMAGEGKTF
VGINLSVMLS LAEKKVLIMG MDLRKPQLAK HFGIEFKDGI TAYLSGQITD YKSMIFSSPE
FPLLDILPAG VIPPNPNELI MKRRFDSLLD ELKEQYDYIV IDSAPVGVVS DSYLIDRVSD
LTLYVCRARY TDKRNIDFIN RIQDEKSLKR LFLVVNDVDL ESNKYAYHRK YGYGYGKNRY
GYGYGYGSKK TDTGKHV
//
