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Database: UniProt
Entry: A0A176L8E7_9ACTN
LinkDB: A0A176L8E7_9ACTN
Original site: A0A176L8E7_9ACTN 
ID   A0A176L8E7_9ACTN        Unreviewed;       653 AA.
AC   A0A176L8E7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=A6P39_09795 {ECO:0000313|EMBL:OAB00769.1};
OS   Streptomyces sp. FXJ1.172.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=710705 {ECO:0000313|EMBL:OAB00769.1};
RN   [1] {ECO:0000313|EMBL:OAB00769.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAB00769.1};
RA   Liu M., Liu N., Shang F., Huang Y.;
RT   "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT   from red soil-derived Streptomyces sp. FXJ1.172.";
RL   Submitted (APR-2016) 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:OAB00769.1}.
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DR   EMBL; LWRP01000056; OAB00769.1; -; Genomic_DNA.
DR   RefSeq; WP_067042511.1; NZ_CP119133.1.
DR   AlphaFoldDB; A0A176L8E7; -.
DR   STRING; 710705.A6P39_09795; -.
DR   OrthoDB; 9762169at2; -.
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-KW.
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: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; 2.
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:OAB00769.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:OAB00769.1};
KW   Transferase {ECO:0000313|EMBL:OAB00769.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        363..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          386..453
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          454..521
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          522..588
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          589..653
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          282..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  68647 MW;  54277645AF3C00A5 CRC64;
     MDTTLQDPLV GQVLDGRYRV DARIAVGGMA TVYRALDTRL DRVLALKVMH PTLAADGTFV
     ERFIREAKSV ARLAHPNVVQ VFDQGADGSY VYLAMEYVAG CTLRDVLRER GALQPRAALD
     ILEPVLAALG AAHRAGFVHR DMKPENVLIG DDGRVKVADF GLVRSVDTVT STTGAVLGTV
     SYLAPEQMEQ GTADPRVDVY ACGVVLYEML TGDKPHSGDS PALVLYKHIH EDVPPPSALV
     PGLPYELDQL VAAATARTPD GRPQDAVALL ARVREARRAL SDEQLDALPP QALSAEHDNA
     GDRTSVIPRS LTSPTLGFAR AGGPPSRPLP VNEDEPASSA GGAVQHTSRL QAPPVPPRRS
     RRLMLTVVAA VLVVFGVGAG VWYINSGQFT KVPPLLSKTE AQARARLETA GLEVGQVRRA
     YNDAVQRGTV ISSDPAPGSR IRDNDSVTLT VSLGPETVNV PDVTGRTLAE ARARLKADGL
     EPGMVTREFS DSVAKGSVIA TAPQAGTKRH AGSAIALTVS KGSPIDVPDV TGDDPADARQ
     QLTDAGLNVV VAPDRVNSEY DKGKVAQQSP GGGSQAAEGD TVTLTLSKGP QMVEVPDVTG
     DSVEDAHKAL EGAGFKVSED RGLLGLFGDT VKKQSVKGGG TAPKGSTITI TIR
//
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