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Database: UniProt
Entry: A0A0P0NCL9_9SPHI
LinkDB: A0A0P0NCL9_9SPHI
Original site: A0A0P0NCL9_9SPHI 
ID   A0A0P0NCL9_9SPHI        Unreviewed;       783 AA.
AC   A0A0P0NCL9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Capsular biosynthesis protein {ECO:0000313|EMBL:ALL04491.1};
GN   ORFNames=AQ505_02680 {ECO:0000313|EMBL:ALL04491.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL04491.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL04491.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL04491.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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; CP012996; ALL04491.1; -; Genomic_DNA.
DR   RefSeq; WP_062546753.1; NZ_CP012996.1.
DR   AlphaFoldDB; A0A0P0NCL9; -.
DR   STRING; 1727164.AQ505_02680; -.
DR   KEGG; pep:AQ505_02680; -.
DR   OrthoDB; 9794577at2; -.
DR   Proteomes; UP000062859; 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   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:UP000062859};
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        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..112
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          436..514
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          579..739
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   783 AA;  86818 MW;  CF499BCB20A3C694 CRC64;
     MKNINSEDKT AHENSDGLDV KQLLLRLLDN WYWIALSVFL CLGLSYLYGK YKTPYYKISA
     RVLVNDEKKG AGMSGGGDLL GDIGGLLGTK STVDNEAEIL KTRNLMAEVV KDMNLNVTYY
     RTGAIKNVEL YESPFQVKVL APVDTIKAAE VKVSFAEKGK VAVTADGLDT LVAFNRSFTI
     PEVGVVQIVE NAAVAPANKN YLFSILSVDS RVIDLMAALT VEVKNKQVTV IDLALNHPVP
     KKGEDILGKL IEKYVQANLK DKNEVADSTV KFIHNRLAHI SGELGGLEGN IQSFKQKNNL
     ADMSEQSKLL VQTSGQYVNE LGKIETQISV LSSLQDYLKD EGKNKKVLPS SLIPTDMVFN
     AVVEKYNALS LERARRMIGV TESNPTIQLM DKEISNARAD IETNIASTLN GFVITRNRIN
     EQMKKAEGQV RNVPQMERSY LNLARQQQIK QELYIFLMQK SEETAISKTA NIANSRTIDP
     PKSEIKAFSP KKAYVYLFGL IAGLAIPLGI MYLKDLLNDK VQLKEDVTKA TKVPVIGEIS
     HQEDNQNMAI ANSSRSAISE QFRALRTNLS FLFKSKNEKV ILFTSSMSGE GKSFVAMNLG
     HILALANKKV LLMELDLRKP GLSAKLNLPG TVGFTNYVAN SEFKTADIIM PLKIQENLFM
     ISSGPIPPNP AELLLSERTQ SLMEELKEQF DYIIIDAPPI GIVTDAQLLA SYADVCIYVV
     RQNYTLKQQL TIVDDLQKSQ KMKGLSLVIN DIKATKGYGY GYTYGDYGTS PQKTGFFNKL
     FKS
//
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