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
//