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Database: UniProt
Entry: F2I6J3_AERUA
LinkDB: F2I6J3_AERUA
Original site: F2I6J3_AERUA 
ID   F2I6J3_AERUA            Unreviewed;       683 AA.
AC   F2I6J3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=HMPREF9243_1559 {ECO:0000313|EMBL:AEA00920.1};
OS   Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC   Aerococcus incertae sedis.
OX   NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA00920.1, ECO:0000313|Proteomes:UP000008129};
RN   [1] {ECO:0000313|Proteomes:UP000008129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002512; AEA00920.1; -; Genomic_DNA.
DR   RefSeq; WP_013669164.1; NC_015278.1.
DR   AlphaFoldDB; F2I6J3; -.
DR   STRING; 866775.HMPREF9243_1559; -.
DR   KEGG; aur:HMPREF9243_1559; -.
DR   PATRIC; fig|866775.3.peg.1465; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_9; -.
DR   OMA; DPDYRYQ; -.
DR   Proteomes; UP000008129; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR017441; Protein_kinase_ATP_BS.
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:SF6; SERINE/THREONINE-PROTEIN KINASE NEKL-3; 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; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AEA00920.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008129};
KW   Transferase {ECO:0000313|EMBL:AEA00920.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          382..448
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          449..516
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          517..585
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          303..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   683 AA;  75316 MW;  0B8D8B6D7DB43A32 CRC64;
     MKQGQVIGNR YEIIRHLGSG GMATVYLAYD PILEREVAIK FLRIGTSDMD DATRRFKREA
     MSISEVNHPN IVNIYDVGDD DDGHYIVMEY IEGIDLKQFI RKNHPISKET YQGIMMQILA
     GVECAHRKGI IHRDLKPQNI MIKPDGQVKI MDFGIALVST ETSITQTNTI IGSVHYLSPE
     QARGSMASYQ SDIYSLGIVS FEMLTGQVPF DGESAVSIAI QHFQESLPDI NQFRSDIPQA
     MQNVIMKATA KEANERYQTC EQMRQDLATC LDPSRANEAP FTPSLMKNET IVMAKDAIEK
     QITDETKVTP QAKPEPKETA QATKAMPIGA GLASQKAEAQ SEAKVKAAPP KASSRSKRRW
     PWFIGGLLAI LLLFGVFVFG QGQSQPVPDL TNMTEDQARN SLVNNGFSLG ESHQEYSDQV
     ESGRVIRTDP SSGRKVKADQ PIDLYISQGK EPIEIPNYQG QTLEQAKKDA EKKGFSVSSE
     EVYSEEVEKG KVISQNPAPG SSVVASETNL HLVVSLGKEP LTMANLQGLN QAGVQQYAQS
     VGLNVSFNEA NSDSVAKGLV VSQSIAPGAN FNRGANLTVT LSLGPEEEPT HSFRHTITIP
     YKGKRSRGDS DSESTSQRQA ANDIEIYIDD LNHSYNEVAD HFTITDDKSY TLSFETEPNK
     TARFKVVRDG KTILENRVKP GDD
//
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