ID I0R1S9_9MICO Unreviewed; 604 AA.
AC I0R1S9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=IMCC13023_02940 {ECO:0000313|EMBL:EIC91815.1};
OS Candidatus Aquiluna sp. IMCC13023.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Aquiluna.
OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91815.1, ECO:0000313|Proteomes:UP000054510};
RN [1] {ECO:0000313|Proteomes:UP000054510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX PubMed=22689238; DOI=10.1128/JB.00586-12;
RA Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT member of the Actinobacteria isolated from an arctic fjord.";
RL J. Bacteriol. 194:3550-3551(2012).
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:EIC91815.1}.
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DR EMBL; AJKR01000002; EIC91815.1; -; Genomic_DNA.
DR RefSeq; WP_007540526.1; NZ_AJKR01000002.1.
DR AlphaFoldDB; I0R1S9; -.
DR STRING; 1081644.IMCC13023_02940; -.
DR eggNOG; COG0515; Bacteria.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000054510; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 2.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 2.
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; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 2.
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:EIC91815.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EIC91815.1};
KW Transferase {ECO:0000313|EMBL:EIC91815.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 340..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..280
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 375..441
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 442..509
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 584..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 604 AA; 63432 MW; 074806F39A6729EC CRC64;
MSKSERLIAG RYRLGELVGR GGMAEVFEGY DTRLGRTVAI KLLKSDLAND ANFEARFRQE
AQASARMAHP TIVRVYDAGE EEAADANGQI VKTPFIIMEL VRGKLLREVV AEKNVAIERT
VGYIAGILTA LEVSHRAGVV HRDIKPANVM VGEGDSIKVM DFGIARAVND NSATQAATAG
IVGTAQYFSP EQARGDAVDA RTDLYSTGVI LYELLAGRPP FKGESAVSVA YQHVSELATP
PSAFNTDVSP ELDAVVLRSM TKDRDERFQT AEEFREHLLA AQAGTALPTT KKVPLSKMTP
VNLDATEVIS TTGGDEFPTS LIEGFETAPS RQITTTTNKV GAGVLWGLGT GVVVILVGLL
FWVMNLGSAG PGTAPSSGVE VASVQGSLYE DAYSTLNSQD LVVLRVYEKS ELVPEGVVIR
QVPEAGTLVL SSTAVTLYVS SGATEVTVPN LVGKNEADAV ALIEGQGLTV GSITVVGSPI
VPDGTVIASD PVTNSKLPLG SVVNIILSDG TVQVPDIRNL EVLEARSILT SPSIGYTVSV
EVLDAETCTG TPGTIVLQQS VLPGEGPQLQ NIILYVECVG GETPAPTPTA TPTPTATPTP
TPVP
//
