ID I7KJU6_9CORY Unreviewed; 804 AA.
AC I7KJU6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Serine/threonine protein kinase, bacterial {ECO:0000313|EMBL:CCI83845.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:CCI83845.1};
GN Name=pknG {ECO:0000313|EMBL:CCI83845.1};
GN ORFNames=BN46_1119 {ECO:0000313|EMBL:CCI83845.1}, HMPREF9719_01380
GN {ECO:0000313|EMBL:EJZ81649.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:CCI83845.1, ECO:0000313|Proteomes:UP000011016};
RN [1] {ECO:0000313|EMBL:CCI83845.1, ECO:0000313|Proteomes:UP000011016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:CCI83845.1,
RC ECO:0000313|Proteomes:UP000011016};
RX PubMed=23045487; DOI=10.1128/JB.01412-12;
RA Brinkrolf K., Schneider J., Knecht M., Ruckert C., Tauch A.;
RT "Draft Genome Sequence of Turicella otitidis ATCC 51513, Isolated from
RT Middle Ear Fluid from a Child with Otitis Media.";
RL J. Bacteriol. 194:5968-5969(2012).
RN [2] {ECO:0000313|EMBL:EJZ81649.1, ECO:0000313|Proteomes:UP000006078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ81649.1,
RC ECO:0000313|Proteomes:UP000006078};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Turicella otitidis ATCC 51513.";
RL Submitted (AUG-2012) 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 -!- 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:CCI83845.1}.
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DR EMBL; CAJZ01000158; CCI83845.1; -; Genomic_DNA.
DR EMBL; AHAE01000067; EJZ81649.1; -; Genomic_DNA.
DR RefSeq; WP_004601270.1; NZ_JH815194.1.
DR AlphaFoldDB; I7KJU6; -.
DR STRING; 29321.AAV33_04605; -.
DR PATRIC; fig|883169.3.peg.1327; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000006078; Unassembled WGS sequence.
DR Proteomes; UP000011016; Unassembled WGS sequence.
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 SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCI83845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006078};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CCI83845.1}; Transferase {ECO:0000313|EMBL:CCI83845.1}.
FT DOMAIN 158..425
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 88888 MW; C3112C2BBB971BAC CRC64;
MSDRQAKRRD TRPEGPAPRR DEVPRDDEAG LVDQPTQAAA YVPTEATAAV SPGGEEPGSA
TQAVRFDPFA DEEDEDDEPR KARQMPQLTS DSHREAISAF RRGATRTSSR TVAEGMVDLP
FIPLVAPADA LIDPEAAARR DGVAPPQLKA GDIVAGQYEI IGTIAHGGMG WIYLANDRNV
AERLVVLKGM QDNLASHDAQ AAAAEREFLA DITHPGIVKI FNFVDDPRIE GGFIVMEYVG
GPSLRDRMRD QPDGLLPVDV AIAYVLEVLP ALDYLHARGV VYNDLKPDNI IVTEDQVKLI
DLGAVSGIGS FGYIYGTKGF QAPDIVTEGP SVESDIYTIG RTLAAMTVRL EVEDGAYAPG
LPSPSEVPLF NRYLAFYRVI ARATHPDPRQ RFHSTNELRN QLYGVLREIL ALRDGRQFPV
QHSVFSPQRR TFGTKHMVFR TDQLIDGTDR SARITAPEVV SALPTPLVDR SDPGAGLLSG
FSYTEPEEAL ERLRQASASE EYTRSTEIPL GIVRTLLDLG LTDRARERLA ELAEELPHDW
RVEWYLGITN LLVDEYPAAQ EHFFRVLRTL PGESAPKLAL AAVDELVLQD QGHDHDAFLD
EQTIRAIAGF NGPVAIPEEA FTDLQEEWGH VMSDPAALRF HAIRLYALVW VTNQQTVSSA
FGLARQLLAE NHIERAVAAL DRVPQASRHH RMAKLTTILQ LVSGELTESR IRRAARRLEE
IPTNEPRFLQ IKTAVLAAGL NFLRDAGVES SASKNKLFDY PFTQTGLRAG IADALRRQAR
GAQFARHRYA LVDMANQVRP VTWF
//