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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//