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Database: UniProt
Entry: A0A2Z6GC47_9PROT
LinkDB: A0A2Z6GC47_9PROT
Original site: A0A2Z6GC47_9PROT 
ID   A0A2Z6GC47_9PROT        Unreviewed;       730 AA.
AC   A0A2Z6GC47;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Tyrosine-protein kinase etk {ECO:0000313|EMBL:BBE51017.1};
GN   ORFNames=OYT1_ch1463 {ECO:0000313|EMBL:BBE51017.1};
OS   Ferriphaselus amnicola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Ferriphaselus.
OX   NCBI_TaxID=1188319 {ECO:0000313|EMBL:BBE51017.1, ECO:0000313|Proteomes:UP000033070};
RN   [1] {ECO:0000313|EMBL:BBE51017.1, ECO:0000313|Proteomes:UP000033070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OYT1 {ECO:0000313|EMBL:BBE51017.1,
RC   ECO:0000313|Proteomes:UP000033070};
RA   Kato S., Itoh T., Ohkuma M.;
RT   "OYT1 Genome Sequencing.";
RL   Submitted (JUN-2018) 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; AP018738; BBE51017.1; -; Genomic_DNA.
DR   RefSeq; WP_062627587.1; NZ_AP018738.1.
DR   AlphaFoldDB; A0A2Z6GC47; -.
DR   STRING; 1188319.OYT1_02487; -.
DR   KEGG; fam:OYT1_ch1463; -.
DR   OrthoDB; 9808257at2; -.
DR   Proteomes; UP000033070; 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, ECO:0000313|EMBL:BBE51017.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033070};
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        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..114
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          390..461
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          531..671
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          264..320
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   730 AA;  79452 MW;  29CF7734E2DC738E CRC64;
     MSEVLHSEKH HSIPSAAHQT DDQLELLVYW RSVVKRKWSI LGLAAAMTLL AAVVVFMMTP
     IYRSTVTILI EQNKTKVVSI EDVYSGIGQG KEYIQTQSEI IKSLSLAKVV VDKLKLTKHP
     EFDPRVNTSW LHSLLATLGA SGKEPTEAEI RDAVAARLAN SLTVEPVKMS QLIKVSFDSP
     DSQLAAKVAN AVAEAFVESD MEAKFQMTQR ASNWLNEHLA GLKVDLQKSE QALQEYRDRE
     HIVDAGNLEL SGASNQLQGL LASLVNARMN RAQAESAYKQ VKNAGDSLES LPVVQKDPLA
     AKLKEVVAEK ERKVSELANR YGKEHVKMIQ AQADLDQARD GLRRHVDVVV AGLQREYEVA
     RANEGALAGA VAEAKGTIQG ANKKGFELSS LERDVATNKQ IYDTFLSRFK ETSATGDSGA
     LVGRVIDPAT PAVSPIKPKK GMVIAVAFVL GLLLGVAVAL LLDRLDNTVR STEDAELKLG
     QPILSTLPLL EGNDDQHMGR YYLDEPRSVF AESVRTARTG VLLSAIDCPN KILVITSSVP
     GEGKTTVSSN LALSHAQTKR VLLIDADMRR PSVAKVMNLD MAKQGLSALV TGTATLEECT
     QTIEGSTLHV VTAGSIPPNP LELLLSNKFE ELLKSLSEKY DMVIIDSPPV QLVSDAVVLS
     TMATGVVFVV KADSTPHQVA RRCIKTLLEA EATLFGVTLN QLDFRKAESY YGAYTGYGKY
     GYDGYYTKET
//
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