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Database: UniProt
Entry: G7ZET3_AZOL4
LinkDB: G7ZET3_AZOL4
Original site: G7ZET3_AZOL4 
ID   G7ZET3_AZOL4            Unreviewed;       774 AA.
AC   G7ZET3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Putative Non-specific protein-tyrosine kinase {ECO:0000313|EMBL:CBS90363.1};
DE            EC=2.7.10.2 {ECO:0000313|EMBL:CBS90363.1};
GN   OrderedLocusNames=AZOLI_p30549 {ECO:0000313|EMBL:CBS90363.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p3 {ECO:0000313|EMBL:CBS90363.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS90363.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p3 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(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; FQ311871; CBS90363.1; -; Genomic_DNA.
DR   RefSeq; WP_014249800.1; NC_016623.1.
DR   AlphaFoldDB; G7ZET3; -.
DR   KEGG; ali:AZOLI_p30549; -.
DR   HOGENOM; CLU_009912_2_0_5; -.
DR   OrthoDB; 230260at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p3.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBS90363.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plasmid {ECO:0000313|EMBL:CBS90363.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBS90363.1};
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:CBS90363.1}.
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..120
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          576..719
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          288..354
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          384..442
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   774 AA;  82790 MW;  78F9605824D46561 CRC64;
     MEAPEHRLPS GAAGFASGLV APPVGSGADK VDVKRLAQTL WRQKWLILGI TAVLWLPAVL
     LINSMTPLYS ASTVVVIDPH PNRVINIPSV SEPMGIYQDT VNTEVEILRS RDLARRVVEA
     LNLGQEPEYA ATAAKPGPLT PLLEDGRALL IDVVGALPEP LSAMLTPPPR PAAPTGDAAE
     MESARLIDAF QKNLRISPGV QSRAIRITVE AKDPQLAARA ANAVADAYIA IQVEAKRNAT
     QRASEWLQSR LDELRQDMTA TGRAAVEAMR SETGMVKGRD APLVNEEMSA LNAQLAEARS
     AHANAQARLR QLQAVRPGDP ESLVGADIGG DPLITGLRQR QAALSAQLAE LRAQYGDRHP
     ALTRPAAELR DLNASLATEV DRVVRGLRGE VEQQVARIQD LSRRLEGLRT ESFDTLQADV
     RLRELQRQAD ASDDNYRRAV TRLKETQVLQ ALEMTPDVRI VSSSSVPTGP VGPGKTVLAG
     LAAVVCGAIA TGIALVRTMG QRGVYSSHQV EALLGLPAVG IVPLLGRTKR GRNAESARDP
     YAETGGSDFA EAVWRLCARL RLVRTGAETA TAKGGEVIML TSSVAGEGKT TLAVALSAFL
     ADAGRRVVVV DCDTRRPAVH RLLGNGRPPK GLTDLLGGDA TLDQVLHLDE RRRVAVIAAG
     RLVDRPQTLL GSQAMLSLLV ELSERYDVIV LDTPPVLSVS DALILAPLAD RILYVVRWAR
     TASSLAGAGI RQVRQVGGRV SGAVLSMVNA REHANLEYGA RPPGGRSYRL RRIA
//
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