ID   Q2W8K0_MAGSA            Unreviewed;       321 AA.
AC   Q2W8K0;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAE49825.1};
GN   OrderedLocusNames=amb1021 {ECO:0000313|EMBL:BAE49825.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE49825.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE49825.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; AP007255; BAE49825.1; -; Genomic_DNA.
DR   RefSeq; WP_011383440.1; NC_007626.1.
DR   AlphaFoldDB; Q2W8K0; -.
DR   STRING; 342108.amb1021; -.
DR   KEGG; mag:amb1021; -.
DR   HOGENOM; CLU_865460_0_0_5; -.
DR   OrthoDB; 9795390at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAE49825.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAE49825.1};
KW   Transferase {ECO:0000313|EMBL:BAE49825.1}.
FT   DOMAIN          31..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   321 AA;  35494 MW;  29173238553943A2 CRC64;
     MPLPLINDYK AAIANAKGRF ATLDVRPHLD ARCSPVFLAG NFAGVFKMVT PEGEHVAVKC
     FTREVSDLPR RYAAVAKFCR TAQCPYVVPL RFLPAEVFVT SSVAPHADYA VVTMPWVEGR
     GLGAVVQILC QRENAPALAG LTRAWSRLCL DLLQRGVAHG DLKHDNVLVG QDGALKLIDY
     DSMYLPELKG LASTMLGGVN FQHPRREVRH FDGTIDHFSM LVILLSLRAL TFQPDLLKRH
     HNGENLVLTK SDFTRPDSSD LLRQWALSPD FHVRDWTEHL IKAAKAPMIG IAAMEALLKA
     AAKVEAVPAK PPTKRLLSFF S
//