ID A0A417D3K6_9FIRM Unreviewed; 746 AA.
AC A0A417D3K6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Stk1 family PASTA domain-containing Ser/Thr kinase {ECO:0000313|EMBL:RHT02608.1};
GN Name=pknB {ECO:0000313|EMBL:RHT02608.1};
GN ORFNames=DW904_04085 {ECO:0000313|EMBL:RHT02608.1};
OS Ruminococcus sp. AM42-11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=2292372 {ECO:0000313|EMBL:RHT02608.1, ECO:0000313|Proteomes:UP000284976};
RN [1] {ECO:0000313|EMBL:RHT02608.1, ECO:0000313|Proteomes:UP000284976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM42-11 {ECO:0000313|EMBL:RHT02608.1,
RC ECO:0000313|Proteomes:UP000284976};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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 -!- 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:RHT02608.1}.
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DR EMBL; QUIO01000004; RHT02608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417D3K6; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000284976; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:RHT02608.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000284976};
KW Transferase {ECO:0000313|EMBL:RHT02608.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 367..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 420..488
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 489..560
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 565..635
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 320..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..418
FT /note="Polar 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 746 AA; 81014 MW; B13D160B107826AB CRC64;
MLKTGMIIVE RYEIVSKIGT GGMADVYKAM DHKLNRFVAV KVLKPEFRED ATFVKKFRSE
AQAAAGLTHP NIVNVFDVGD DEGVYYIVME LIEGITLKEY ISKKGKLSVK EATSIAIQVS
MGLEAAHSHG IVHRDVKPQN IIISTDGKVK VTDFGIARAA SSNTISSNVM GSVHYSSPEQ
VRGGYSDEKS DIYSLGITLY EMVTGRVPFD GDTTVAIAIK HLQEEMVPPS VYSPDLPYSL
EQIIMKCTQK SVDRRYNKME DVIEDLKHSL IDPQGDFVKL TSVDTDAKTV VISDEELGEI
KHTPKQTLKP DIETLEKELN ETNYDDDDDF GYDDKEESSK GSRKNRDRER SREREERERR
IKKQKRGVSV AGSIIALIIG AAVLIAVILV VGKAAGLIGD SKDSSLDQQN QQAQVTQAAD
EDDGMVPVPD LIGKTEAEAQ ELCASVNIGM TYKGEEASTQ EKGKISSQDP VQGTKVAKNS
TVNYYLSKGS ESVTLTDMFG QNGALAQETL ESQGLTVQIN KIYPDESQSS MVDIGCVLDT
EPAAGTTVKA GDTVTLTISR GINYGDSVQV PDVTGMEKND AIAKLGKFIN INVEMQMSTD
VAEGTVISQD PIGYTDDNPV YADPDNDTIT LIVSSGSQDT SSQNTEDQSS SDTTAAANGE
VWKCTQKLNT PTGYNGGLIR LELVQNVGGA PKASSVVEGQ QLTFPYQLDI TGAPGVAEGT
LYLSEQQSDG SYQELGHYPL TFEKVE
//
