ID A0A1J0GG29_9CLOT Unreviewed; 498 AA.
AC A0A1J0GG29;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:APC39854.1};
GN ORFNames=A7L45_07115 {ECO:0000313|EMBL:APC39854.1};
OS Clostridium estertheticum subsp. estertheticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1552 {ECO:0000313|EMBL:APC39854.1, ECO:0000313|Proteomes:UP000182569};
RN [1] {ECO:0000313|Proteomes:UP000182569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX PubMed=27891116;
RA Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA Bolton D., Fanning S.;
RT "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT Identified in Spoiled Vacuum Packed Beef.";
RL Front. Microbiol. 7:1764-1764(2016).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR EMBL; CP015756; APC39854.1; -; Genomic_DNA.
DR RefSeq; WP_071612148.1; NZ_CP015756.1.
DR AlphaFoldDB; A0A1J0GG29; -.
DR STRING; 1552.A7L45_07115; -.
DR KEGG; ceu:A7L45_07115; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000182569; 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 CDD; cd06577; PASTA_pknB; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000182569};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 346..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 394..461
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 498 AA; 54981 MW; 05DC8E043ABE9329 CRC64;
MIGTFLLNRY ELLENIGEGG MGTVYKAKCH VLNRFVAVKI LKSELSNDDE FVSRFKMEAT
SIAKLSHPNI VNVHDVCSEN DVNFIVMEYV DGKTLKQIIK ENGRITSKET LDIVFQVAKA
LQCAHTSGII HRDIKPDNIM ITKEEMVKVM DFGIAKVADA RTVTNSNKVM GTAHYFSPEQ
AKGNFVDCRS DIYSLGIVMY EMVTGKVPYD AESAITIAML HIQGVIIAPK DVIINIPENI
NQVILRAMQK ETIERYQTAN EMAEIIGAIK ENPNYKVIVN SEIDGATKIM DTVVASNIRD
DLTTVMSKEE IFDKTVFGKP LAEETILKKE SEVIPIKKKI SRNKKVIIII MSIILIVSIV
ALGKSLANGN VIEDKATINT KATVVKTIVP KVQVFEKKFV PSLIGKTQDS ARQVAVSNGF
LLGDITSNYS DSIDKGLVIS QSPVVNTAYE KGGKISIVLS LGKDKVQATP PQTKVVKDMK
KIEQIHGKSP KGKHSKNK
//
