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Database: UniProt
Entry: Q6AE50_LEIXX
LinkDB: Q6AE50_LEIXX
Original site: Q6AE50_LEIXX 
ID   Q6AE50_LEIXX            Unreviewed;       633 AA.
AC   Q6AE50;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pkaF {ECO:0000313|EMBL:AAT89346.1};
GN   OrderedLocusNames=Lxx15400 {ECO:0000313|EMBL:AAT89346.1};
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=281090 {ECO:0000313|EMBL:AAT89346.1, ECO:0000313|Proteomes:UP000001306};
RN   [1] {ECO:0000313|EMBL:AAT89346.1, ECO:0000313|Proteomes:UP000001306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07 {ECO:0000313|EMBL:AAT89346.1,
RC   ECO:0000313|Proteomes:UP000001306};
RX   PubMed=15305603;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT89346.1; -; Genomic_DNA.
DR   RefSeq; WP_011186336.1; NC_006087.1.
DR   AlphaFoldDB; Q6AE50; -.
DR   STRING; 281090.Lxx15400; -.
DR   KEGG; lxx:Lxx15400; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   Proteomes; UP000001306; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AAT89346.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001306};
KW   Transferase {ECO:0000313|EMBL:AAT89346.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        337..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          360..427
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          499..565
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          566..632
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
SQ   SEQUENCE   633 AA;  66380 MW;  70084F63890682A5 CRC64;
     MTTSQTDPLI GRLIDGRYQV RSRIARGGMA TVYLATDLRL ERRVAIKVMH GHLADDTTFK
     NRFVQEARSA ARLAHPNVVN VFDQGQDSDM AYLVMEYLPG ITLRDLLKDY GKLTPEQTID
     IMEAVLSGLV AAHKAGIVHR DLKPENVLLA DDGRIKIGDF GLARAASANT ATGQALLGTI
     AYLSPELVTR GVADARSDIY ALGIMMYEML TGEQPFQGEQ PMQIAYQHAN DAVPTPSGKN
     PAVPAELDDL VQWATEKDPD RRPKDARELF DRLVEAEKSL RGEAALQLTM VLPPAFEAAE
     GETQIINPAI RQQVAASAPS ATDRLSAASA RRRAKGWWLF ALVILLAGLA GGTGWYFGAG
     PGSLVTVPNV VSKTPAAAAA KLTELGFRTK QAQEYSVTVP AGQVSSTVPV AETPAGRGST
     VTLRVSQGPK PVTIPPLAGH PLDTAKAAIT GVGAKVGTIA EQFDGKVHSG TVISATKTSD
     GGDISGGGPY FEAASVDLVV SVGPVPDVAG KSVESATALL HKAGLVVVAG PESYSETIAK
     GDVISAQPQA AVVRPGDTVA LKTSKGPEPV PVPDVVGQTW DKAKKTLTEA GFALKYSTAA
     DLLPGAFVVS KISPDAGTQA DKGSTVTVNF ASF
//
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