ID A0A135L420_9BACI Unreviewed; 637 AA.
AC A0A135L420;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXG43716.1};
GN ORFNames=U473_06575 {ECO:0000313|EMBL:KXG43716.1};
OS Tepidibacillus decaturensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG43716.1, ECO:0000313|Proteomes:UP000070352};
RN [1] {ECO:0000313|EMBL:KXG43716.1, ECO:0000313|Proteomes:UP000070352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z9 {ECO:0000313|EMBL:KXG43716.1,
RC ECO:0000313|Proteomes:UP000070352};
RA Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT Subsurface of the Illinois Basin, USA.";
RL Submitted (FEB-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:KXG43716.1}.
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DR EMBL; LSKU01000001; KXG43716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135L420; -.
DR STRING; 1413211.U473_06575; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000070352; 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:0010506; P:regulation of autophagy; IEA:InterPro.
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; IPR045269; Atg1-like.
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; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR PANTHER; PTHR24348:SF77; SERINE_THREONINE-PROTEIN KINASE DDB_G0271538-RELATED; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000070352};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 350..416
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 417..487
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 488..555
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 637 AA; 72304 MW; 85A1AC0226600C5E CRC64;
MIGILLANRY KIVEKIGGGG MADVFRAIDE VLQEEVAVKV LRQQYVHDDD FVKRFRREAH
SVASLSHENV VKIFDIGEEK EIYYIVMEYV KGSTLKEVIQ RKGKLSIKEA LKIAEQIALA
LDHAHQHHII HRDIKPHNIL IGNQGQVKVT DFGIARAVSS ATITQAGSVL GSVHYLSPEQ
ARGGWTDEKT DLYSLGVVLY EMITGSLPFS GDSPISVALK HLQENFIYPR ELDPSIPQSV
ENIILRALMK DPLKRYASAE EMFKDIKTAL DPKRIHEPRI LLETDVFDDD EENTITIPAM
KEFNANDAYS TQSRKNKKRS LRPKLVPILT IFFLLLLGVF GFQYISSKLV VPEIEAPLLE
GKSKEDAIKL LQELNLTYKI EEKTDPVVEK GKVIKQEPYP GETMKTSQSI TLYISLGKEK
VAMPNLLNKQ QRQAKIFLQQ LGFNENHIEI KKEFNNEVPS GEVFKQEPNA EEMVVPDEQK
VILFISEGKE QLKMPNLIGR DEAEAVAMVT AIGLVPRVQK DYSYQQPEGK VYRQFPFDPN
QEVTAGDQVD IYVSLGYPKE LKSIYSDLLV DLEEDESAEI TIILRDARGT DVIWKKETIT
GPKFYDNIEL LLLPDQQGTI NVYKNGKLVK MKTVQYY
//
