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Database: UniProt
Entry: A0A1H0S818_9MICO
LinkDB: A0A1H0S818_9MICO
Original site: A0A1H0S818_9MICO 
ID   A0A1H0S818_9MICO        Unreviewed;       569 AA.
AC   A0A1H0S818;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Non-specific protein-tyrosine kinase {ECO:0000313|EMBL:SDP37900.1};
GN   ORFNames=SAMN04489867_2245 {ECO:0000313|EMBL:SDP37900.1};
OS   Pedococcus dokdonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Pedococcus.
OX   NCBI_TaxID=443156 {ECO:0000313|EMBL:SDP37900.1, ECO:0000313|Proteomes:UP000199077};
RN   [1] {ECO:0000313|Proteomes:UP000199077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; LT629711; SDP37900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0S818; -.
DR   STRING; 443156.SAMN04489867_2245; -.
DR   OrthoDB; 9812433at2; -.
DR   Proteomes; UP000199077; Chromosome i.
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, ECO:0000313|EMBL:SDP37900.1};
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,
KW   ECO:0000313|EMBL:SDP37900.1}.
FT   TRANSMEM        14..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..90
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          261..399
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          460..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  59784 MW;  E15C6E464B1B914A CRC64;
     MTLRAYLQIL LKRWRIVVAC LVLVLGSAGT LTYLTPPTYA AYATAFVSIS QAGTADASIY
     QSSQFAMQRV KSYTEVVKSP DVLQPVIDDL DLDMSVSDLR QVVAAENPVD TVLIKISATD
     AKASRAQAIA NAVSDQLGLV IERLETPREG GQSPVKVTTT VPSALPRSPI SPRIPLNMAL
     GLLAGLALGV IVAVIREQQD TTVKGDELEE LTGRAALALI GLNPAVKTQP LITMQGHGRG
     VEEFRSLRTT LQFVDVDQPP RVIVITSALA AEGKTTTACN LAIALAQSSL RVCLVEADMR
     RPNAATLLGV DGSIGLSNVV AGQIDLADAL MPWHRGLLTI LPAGTTPPDP TRLLGSKNMA
     AVLATLRADF DFVIIDAPPI LPVSDAAVLA RAADGAVLVA RYGKTRREQL TSAIADLEAV
     KARLIGTALT MVPARGQRDL RGHDEDYAAI AAVSENDWPA AAIPTAPNDG SVADDTKPVA
     PTSPAPREPS TDDAGGGTAK DTRGSDGSSA PERDRNGAGD RDRGGRDRDR GDDRGNRDGR
     QGAPVSLDPR VVGTSFSKAM KPSGQGRVH
//
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