ID A0A498EAI2_9ACTN Unreviewed; 668 AA.
AC A0A498EAI2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknB {ECO:0000313|EMBL:RLL67804.1};
GN ORFNames=D7M15_14225 {ECO:0000313|EMBL:RLL67804.1};
OS Streptomyces sp. Z26.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2500177 {ECO:0000313|EMBL:RLL67804.1, ECO:0000313|Proteomes:UP000288048};
RN [1] {ECO:0000313|EMBL:RLL67804.1, ECO:0000313|Proteomes:UP000288048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z26 {ECO:0000313|EMBL:RLL67804.1,
RC ECO:0000313|Proteomes:UP000288048};
RA Buchmann A., Cano-Prieto C., Baz M., Hassani L., Barakate M., Nafis A.,
RA Niedermeyer T.H.J., Gross H.;
RT "Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces
RT sp. Z26, isolated from potato rhizosphere in Morocco.";
RL Submitted (OCT-2018) 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:RLL67804.1}.
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DR EMBL; RCHV01000002; RLL67804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498EAI2; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000288048; Unassembled WGS sequence.
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; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
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:RLL67804.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000288048};
KW Transferase {ECO:0000313|EMBL:RLL67804.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..438
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 439..503
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 504..570
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 582..645
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 299..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..633
FT /note="Polar residues"
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 668 AA; 71073 MW; 2FB5AEDFC1D8596D CRC64;
MEEPRRLGGR YELGSVLGRG GMAEVYLAHD TRLGRTVAVK TLRVDLARDP SFQARFRREA
QSAASLNHPA IVAVYDTGED YVDQVSIPYI VMEYVDGSTL RELLHSGRKL LPERSMEMCV
GILQALEYSH RNGIVHRDIK PANVMLTRGS QVKVMDFGIA RAMGDAGMTM TQTSSVIGTA
QYLSPEQAKG ESVDARSDLY STGCLLYELL TVRPPFIGDS PVAVAYQHVR EEPQPPSSFD
PEITPEMDAI VLKALTKDPD YRYQSADEMR ADIEACLDGQ PVAATAAMGA VGYGGYGDEQ
PTAAIRPQDQ NHTSMLPPMR DDDGGYYGDE PRGRRRTQKK NNTSTVLLVA ALVLVLVGAV
FIGNALWGGD KDSGDVVVPE LAGKTLEEAE QLGDNGDFTI EKGQSKYCDQ KKSTICESTP
AAGEKIEHGA AVTVALSKGA APVEVPDVEG DDFDKAEQEL EDAGFEVKRK NEESDADEGS
VIGQDPAGGD KARKGSTITL TVATQQQTSV PNVVDKDFEE AKAQLEGLGF TVAKVEQDAP
GKEPNKVIKQ DPAPPSKAPE GGQVTLTVAK APAEDEDPPE DDKPVNVPDV SNQLVRDARG
ALEGAGFKVE VQGAPDENNA TVLTTNPGPN TPAKKGDTVT IIARPGAPGG GPGGGDNGGF
PFGGLRGD
//
