ID A0A077HMC2_9CORY Unreviewed; 793 AA.
AC A0A077HMC2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AIL97564.1};
GN ORFNames=CUREI_10005 {ECO:0000313|EMBL:AIL97564.1};
OS Corynebacterium ureicelerivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL97564.1, ECO:0000313|Proteomes:UP000028939};
RN [1] {ECO:0000313|EMBL:AIL97564.1, ECO:0000313|Proteomes:UP000028939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL97564.1,
RC ECO:0000313|Proteomes:UP000028939};
RA Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT patient.";
RL Submitted (AUG-2014) 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; CP009215; AIL97564.1; -; Genomic_DNA.
DR RefSeq; WP_038613092.1; NZ_CP009215.1.
DR AlphaFoldDB; A0A077HMC2; -.
DR STRING; 401472.CUREI_10005; -.
DR KEGG; cuv:CUREI_10005; -.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000028939; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AIL97564.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028939};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AIL97564.1}; Transferase {ECO:0000313|EMBL:AIL97564.1}.
FT DOMAIN 143..388
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87013 MW; 907B6A40E636628B CRC64;
MSDTPEETQP TEAVAFDPFA DDEEPATEAV AFDPFADEDE DEAETDYSAM GEMAGLLQDL
DKLRKGGKHD DTSQRSRRQA LDTFRERRGA RRVTRVVADG MVELPWVEPT QPKEALIDPE
PAVVRKGLTP PVLQPGDVVA GQYEIMGVIA HGGMGWIYLA QDHYVAGRVV VLKGLHSTEN
PDEAAAAAAE REFLADITHP GIVQIFNFID DPRVPGGFTV MEYVGGPSLR AWRNASKSGV
LEPDIAIAYL LEVLPALDYL HSRGVVYNDL KPDNIIVTED RVTLIDMGAV SGIGAFGFIY
GTKGFQAPEV ASQGPSIASD VYTVGRTLAS LVVDLPQTDG VYDAGIPTPA EEPLFRQYTS
LYRLIARCCD EDPARRFTTL PELEAQLLGV LREVVAVRDG RTFPAQHSLF SPQRTTFGTK
HLVFRTDQLI DGIARSVDIT PQEVVAALPS PLIDRSDVGA AMLQGSSYAE PRETLEMLRQ
AMSTPQYERS VEIPFGVVRT MLDLGLTGQA RAWLRSLSER FGSNWRYCWY AGVVETLLGN
FDAAKNSFAQ VLYQLPGEAA PKLALAAISE LILQDEGLQD SELLDDELAP AAAGLAQHLC
DVPDSAFEQM AASGVTDATW SMHTLSPEGL RFHAIRLYAL VWLTNPTTVS SAFGLARMLM
CEREVDLAIK ALDKVPGASR HSRMAQLTAI LCLVAGQPTE AQIRLAARRL EQIPSTEPRF
LQIKVSVIEA GLTHLREYGS AGPAPLFEYP FTMRELRRGL AHTLRAQARI APYPRHRYAL
VDMANKVRPA TWF
//