ID   PTK_ACIJO               Reviewed;         733 AA.
AC   O52788;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tyrosine-protein kinase ptk;
DE            EC=2.7.10.-;
GN   Name=ptk;
OS   Acinetobacter johnsonii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=40214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=9434192; DOI=10.1016/s0378-1119(97)00554-4;
RA   Grangeasse C., Doublet P., Vaganay E., Vincent C., Deleage G., Duclos B.,
RA   Cozzone A.J.;
RT   "Characterization of a bacterial gene encoding an autophosphorylating
RT   protein tyrosine kinase.";
RL   Gene 204:259-265(1997).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=8683591; DOI=10.1006/jmbi.1996.0366;
RA   Duclos B., Grangeasse C., Vaganay E., Riberty M., Cozzone A.J.;
RT   "Autophosphorylation of a bacterial protein at tyrosine.";
RL   J. Mol. Biol. 259:891-895(1996).
RN   [3]
RP   MUTAGENESIS OF LYS-436; LYS-549; SER-550 AND ASP-651.
RX   PubMed=10069388; DOI=10.1016/s0014-5793(99)00111-8;
RA   Doublet P., Vincent C., Grangeasse C., Cozzone A.J., Duclos B.;
RT   "On the binding of ATP to the autophosphorylating protein, Ptk, of the
RT   bacterium Acinetobacter johnsonii.";
RL   FEBS Lett. 445:137-143(1999).
CC   -!- FUNCTION: May be involved in the production and the transport of
CC       exopolysaccharides.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC   -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- PTM: Autophosphorylated on several Tyr residues. Dephosphorylated by
CC       ptp.
CC   -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
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DR   EMBL; Y15162; CAA75431.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52788; -.
DR   SMR; O52788; -.
DR   KEGG; ag:CAA75431; -.
DR   BRENDA; 2.7.10.1; 103.
DR   UniPathway; UPA00631; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR005702; EPS_synthesis.
DR   InterPro; IPR032807; GNVR.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13614; AAA_31; 1.
DR   Pfam; PF13807; GNVR; 1.
DR   Pfam; PF02706; Wzz; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01007; eps_fam; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane;
KW   Exopolysaccharide synthesis; Kinase; Magnesium; Manganese; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   CHAIN           1..733
FT                   /note="Tyrosine-protein kinase ptk"
FT                   /id="PRO_0000212352"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         542..550
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         436
FT                   /note="K->M: No loss of autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:10069388"
FT   MUTAGEN         549
FT                   /note="K->M: Loss of autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:10069388"
FT   MUTAGEN         550
FT                   /note="S->C: Loss of autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:10069388"
FT   MUTAGEN         651
FT                   /note="D->N: Loss of autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:10069388"
SQ   SEQUENCE   733 AA;  82362 MW;  EF3148A2AFF7B954 CRC64;
     MYVMSQTTNT EDTIDLKELF FSLIAQWKLI ALCIILSLIC ALLYLRATPD TYSVNALVQV
     EENKGASAAL LGDLSSMIEQ KQPAQAEIEI LKSRLVLGNV IQHLNLDLKI SGTENSFTDR
     LLSPHHYQTE YQPKSVLFKD DEKVFDIRQF NIPASFRDKK IELRFKDGQF SLTNTQTEQV
     ILTGKTNQSN TLRTADGLWN ISIYTQDQLN DVYLIQKQSL PAAVNNILTN YSVAEKGKLT
     GILGLNYQGT DKTHITQVLN AILVSYSQQN IERRSAETAQ TLKFLDEQLP ELKQQLDVAE
     REFNKFRQQY NTVDVTKESE LFLTQSVTLE TQKAQLEQQV AEAGAKYTSE HPVMKQMNAQ
     LGAINKKIGE LNATLKELPD LQRRYLQLYR EVEVKQQLYT ALLNSYQQLR IAKAGEIGNV
     RIVDTAVEPI EPIAPKKLQI LILSIFLGGF LGTLLALLRN MMRSGIKDST QIENELDLPV
     YATVPRSPVQ ESRINILKKK KNIPILAVKN SDDIAIESLR SMRTAIHFAL SSARNNLITI
     SGPAPEVGKS FISTNLATIL AQSDKRVLII DADLRRGYLH KYFNLDTQPG LTELLNGQQS
     LETVIRHTEV PGLSVISRGK SPANPSELLS SNQFKNLLEQ MSEKFDHVII DTPPVLAVTD
     GIIISQYTGV NLVIARYAKT QMKELELTLN RFEQAGVKVN GFILNDIQRS SAGYGYGYGY
     NYAYAYKANK ESD