ID A0A0S9R7I7_9ACTN Unreviewed; 590 AA.
AC A0A0S9R7I7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=ASF37_05490 {ECO:0000313|EMBL:KQP78063.1};
OS Aeromicrobium sp. Leaf289.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP78063.1, ECO:0000313|Proteomes:UP000051640};
RN [1] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQP78063.1}.
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DR EMBL; LMNK01000002; KQP78063.1; -; Genomic_DNA.
DR RefSeq; WP_056579420.1; NZ_LMNK01000002.1.
DR AlphaFoldDB; A0A0S9R7I7; -.
DR OrthoDB; 9769043at2; -.
DR Proteomes; UP000051640; 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 CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000051640};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 359..425
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 426..491
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 492..556
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 388..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 590 AA; 61910 MW; F55CADAFA6215BC1 CRC64;
MTGTPDEPIL LGERYELGGL LGRGGMADVR VARDLRLGRT VAIKQLRADL SSDDTFQARF
RREAQSAAAL NHPAVVAVYD TGDSTDKHGN HIPYIVMEYV EGQTLREILR DDRKILPERA
LSITADVLSA LDYSHRSGII HRDIKPANVM LTPSGQVKVM DFGIARAIAD SSSAMTQTAA
VIGTAQYLSP EQARGETVDA RSDIYSTGCL LYELLTGRPP FVGDSPVSVA YQHVREEARP
PSQLNPDVSQ PVDHIVAKAL AKRTDDRYQS AADMRKDLER AIAGQHVDAP TQATSAIPAA
TAVAPAVAAA AATGTQPAVA DDEEEEKKNK ALWWALGILA ALIIAGLAYF LLAGNDTEDP
AQVRVPDVVG QDAVAAQRTL EGEGFTVTTE ERPDADVESG DVVSQTPEGD SMAPDGSEIE
LIVSSGPEQV QVPNVVGLNY DEAKDALEGE GLKVKKEERA SDESKDTVIN TNPPAGQSVD
VGATVTVIVS EGEVTVPNVI GMSRDEAQKA LEDLDLEVSV TEDPSSSAPE DEVTGQSTPA
GQTVPPGSSI EITVSSNPGD DGGPGNGDAD ANGEADADAG ADGVADGLGQ
//
