ID F9DPF7_9BACL Unreviewed; 654 AA.
AC F9DPF7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Non-specific serine/threonine protein kinase {ECO:0000313|EMBL:EGQ27239.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:EGQ27239.1};
GN ORFNames=HMPREF9372_0687 {ECO:0000313|EMBL:EGQ27239.1};
OS Sporosarcina newyorkensis 2681.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1027292 {ECO:0000313|EMBL:EGQ27239.1, ECO:0000313|Proteomes:UP000005316};
RN [1] {ECO:0000313|EMBL:EGQ27239.1, ECO:0000313|Proteomes:UP000005316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2681 {ECO:0000313|EMBL:EGQ27239.1,
RC ECO:0000313|Proteomes:UP000005316};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (APR-2011) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:EGQ27239.1}.
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DR EMBL; AFPZ01000019; EGQ27239.1; -; Genomic_DNA.
DR RefSeq; WP_009765554.1; NZ_GL982997.1.
DR AlphaFoldDB; F9DPF7; -.
DR STRING; 759851.SAMN04244570_2440; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000005316; 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; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.40.2560; -; 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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF21160; PrkC-like_PASTA-like; 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; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EGQ27239.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EGQ27239.1};
KW Transferase {ECO:0000313|EMBL:EGQ27239.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..267
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 353..420
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 421..488
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 489..556
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 654 AA; 73705 MW; 430F05C395AFD179 CRC64;
MIGKRIGKRY EIIRVIGDGG MSRVYLAHDM ILDRDVAIKV LHYDFANEEE LKKRFQREAL
SATSLTHPHI VNIFDVGQED ELHYLVMEYI PGRTLKEYIH THGALSADHA VSIMQQLVSA
ISHAHHNGIV HRDIKPQNVL INGEDDVKIT DFGIAMALNS TAHTKTNSVI GTVHYLSPEQ
ARGGMATKRS DIYSLGIVFY ELLTGKLPFS AETAVAIALK HLQEETPSVR EQLPEIPQTV
ENVILKATAK DANYRYATAD EMYDDLLTVF SPERANDKKF TLPFDDDRTV AIPIVKDTSK
FDNVENTVKH SPAAVGPVPP DEKKKKKKKW PLIVGASLLF IAVLAVALTM WLKPKEIIVP
EVIGEEELAA TELLEKEGFV IDERLEETSD EFNAGQVIKT VPEAGKKRKE GDGVKLFVSI
GKDKMKLLNY VGRSYEATVQ FLENYGFEKI TPVEEYSDEP KGTIIGQQPE ADQEVVPEET
EIIFTVSKGK ELHSLNDLSG MTKSQLESYA KSSGLNIHIV SEEYSEKVEK GRVISQRPSK
GTKMDKNERV DVVMSKGAPS KPVKLLVKTI LIPYEGREGE NEWGEEVERE PQKIQIYIQD
RKRTMNDPVE EFEITEDTSR KITIELEEGE RGGYKVLRNQ TVIEEDKFDY KELN
//
