ID A0A3N2P9D6_9ACTN Unreviewed; 669 AA.
AC A0A3N2P9D6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:ROT31267.1};
GN ORFNames=EF879_16840 {ECO:0000313|EMBL:ROT31267.1};
OS Micromonospora sp. HM5-17.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2487710 {ECO:0000313|EMBL:ROT31267.1, ECO:0000313|Proteomes:UP000281230};
RN [1] {ECO:0000313|EMBL:ROT31267.1, ECO:0000313|Proteomes:UP000281230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM5-17 {ECO:0000313|EMBL:ROT31267.1,
RC ECO:0000313|Proteomes:UP000281230};
RA Thawai C.;
RT "Micromonospora sp. HM5-17, a new actinomycetes isolated from a hot spring
RT soil.";
RL Submitted (NOV-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:ROT31267.1}.
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DR EMBL; RJWA01000005; ROT31267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2P9D6; -.
DR OrthoDB; 308915at2; -.
DR Proteomes; UP000281230; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ROT31267.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000281230};
KW Transferase {ECO:0000313|EMBL:ROT31267.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 410..473
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 474..541
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 542..607
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 608..669
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 335..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 71822 MW; 059130DBB4838618 CRC64;
MDNQVADTLL NALIDGRYRI RGRVARGGMA TVYTATDERL DRTVAIKIIH PHQANSARVQ
VAEFLARFTD EAKTIARLTH PNVVAVYDQG TYNGVPYLVM EYVRGRTLRD ILTERGRLNP
SEALAIMEQM LAAIAAAHRA GLVHRDVKPE NVLVAEAPSG GRTNLVDSVV KVADFGLARA
VEASSETDGA NQLMATVAYV APELVTEGRA DPRTDVYSAG IVLFEMLTGR VPYDAERALD
VAWQHVDRDV PRPSTLVPGL PPVLDDLVVR ATRRDPGARP TDAGALQAEV QVVRDDLGTM
ANASTTVLRP VPTPLEQPTM VVQQPTMVVS TVPPAERPSW ARLPEQPRER STPHRRRAAP
PRDGAAGRLA DLRERLLADR TSRVAVGAAV LALILVIAGV GWWFGAGRYT STPNLINLAG
TEAQARAERA GFEVAFTAPR YSNEVAKDAV LAQDPTSDER IVRGGTITLT LSLGPERFPV
PDVVGKTLDL AQLDLEEAGL KVKRGPDRYD DNLEKGVVVA VDPEVGTEVK PGDTITVIVS
KGKAPITVPV LIGKSLAEAR TALQQLNLEI VVEYKESDRP KDEVLAQNPP DGAGVEPGAK
VTVEVSEGPP LVTVPSVMNL PCPQARQILE GAGLTVGGLH INPNGPVRSQ NPAPNTQVPP
RTQVAITCF
//
