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Database: UniProt
Entry: A0A0R2GYI3_9LACO
LinkDB: A0A0R2GYI3_9LACO
Original site: A0A0R2GYI3_9LACO 
ID   A0A0R2GYI3_9LACO        Unreviewed;       639 AA.
AC   A0A0R2GYI3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=IV41_GL001115 {ECO:0000313|EMBL:KRN45374.1};
OS   Limosilactobacillus ingluviei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN45374.1, ECO:0000313|Proteomes:UP000051639};
RN   [1] {ECO:0000313|EMBL:KRN45374.1, ECO:0000313|Proteomes:UP000051639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN45374.1,
RC   ECO:0000313|Proteomes:UP000051639};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRN45374.1}.
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DR   EMBL; JQBA01000003; KRN45374.1; -; Genomic_DNA.
DR   RefSeq; WP_056993713.1; NZ_JQBA01000003.1.
DR   AlphaFoldDB; A0A0R2GYI3; -.
DR   STRING; 1203076.GCA_000312405_00782; -.
DR   PATRIC; fig|148604.4.peg.1152; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000051639; Unassembled WGS sequence.
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; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.40.2560; -; 1.
DR   Gene3D; 3.30.10.20; -; 3.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KRN45374.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051639};
KW   Transferase {ECO:0000313|EMBL:KRN45374.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        336..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..281
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          421..488
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          489..555
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
SQ   SEQUENCE   639 AA;  70667 MW;  28C95E41D3D403AC CRC64;
     MKSGYKLNNR YRILRPLGEG GMANVYLAYD QVLERKVSVK LLRMDLRDDP KTQRRFEREA
     MAATQLNDPH IVGVYDVGTD HGMQYMVMQY VEGTDLKAFI KQNYPIPLPQ VVDIMEQVLA
     AVETAHRHGI IHRDLKPQNI LIDEDKNIKI TDFGIAMAST ANSLTQTNTL VGSVHYLSPE
     QARGSIATER SDIYSLGIIL FELLTGHVPF EGETAVSIAL KHFRDEMPSV RDINPAIPQP
     LANVVYKATA KSPQQRYESA AAMAADLKTA LNPGREAEPR FQEHDACDDQ TRVLDLAELK
     AADHQAQQQL AQDDSEEDTK QLAPLPTKAH SNWLRGLLVA LAVVIVMALG GLWYFNRPIA
     VPSVAGKTPV QASRVLAHHH LKIGTITREN SATVAKGKVI KSASAAKVRY GRAVNLVVSD
     GVAHWKMKDL VGTDVDQAQQ QLENLGFTVK IQKKHSDEIA EGQIIKQNVT AGKTIQPTKQ
     VVTLTVSAGR KQIKIPNFKN KDIKDVQAFA NEHGLQLTET KKKSTTVATN RVLAQTPKTG
     STLAQGDTLT VTVATSGDQL KTTNIQISIP FDSNNGRKEN RVQVYISDAY HNLTMEYEDI
     TINQETVIYV PFTLRDNQMG AYKVIRNGRT IMSATNITG
//
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