ID Q5FJH8_LACAC Unreviewed; 674 AA.
AC Q5FJH8;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Serine-threonine protein kinase {ECO:0000313|EMBL:AAV43146.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:AAV43146.1};
GN OrderedLocusNames=LBA1317 {ECO:0000313|EMBL:AAV43146.1};
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN [1] {ECO:0000313|EMBL:AAV43146.1, ECO:0000313|Proteomes:UP000006381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC {ECO:0000313|Proteomes:UP000006381};
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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};
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DR EMBL; CP000033; AAV43146.1; -; Genomic_DNA.
DR RefSeq; WP_011254416.1; NC_006814.3.
DR RefSeq; YP_194177.1; NC_006814.3.
DR AlphaFoldDB; Q5FJH8; -.
DR STRING; 272621.LBA1317; -.
DR GeneID; 56942903; -.
DR KEGG; lac:LBA1317; -.
DR PATRIC; fig|272621.13.peg.1247; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR BioCyc; LACI272621:G1G49-1296-MONOMER; -.
DR Proteomes; UP000006381; Chromosome.
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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-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; 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}; Kinase {ECO:0000313|EMBL:AAV43146.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006381};
KW Transferase {ECO:0000313|EMBL:AAV43146.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 360..427
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 428..495
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 502..568
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 589..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..617
FT /note="Basic and acidic 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 674 AA; 74824 MW; 8A2A60B03AAE6174 CRC64;
MIDKGYLLGE RYRIIDTLGE GGMANVYLAE DIILQRKVAV KILRLDLQNE SQTQARFQRE
ALATSELSHP NIVSVLDVGT DHGLPYMVME YVDGPDLKDY IRENSPLDLR EVIQIMDQIL
SAVALAHKHN VIHRDLKPQN ILMDKRGNIK IADFGIAVAL NQSSITQTNS VMGSVHYMSP
EQTRGGLVTR QSDIYSLGII LYELITGTVP FNGDTPVSIA LKHAQEPIPS IRKKDRSVPQ
ALENVVLKAT AKDPRDRYPS AQAMKADLDS SLDPARADEP VFVPTHGNND DKTIVLPGFK
PQKDPAPETE KEEVVSSEKE DKTSFWQNVK KHKWWWIFSI IAAGLIIFIM IFALSGNSNK
PTQVNIPDVT NVAEKEAENR LKAAGLQVGR IIRRQSDDVK KGYVIATRPT AGNSVNKGNS
VNLIVSSGSS MVKVPDVVGD RYDEAAEKLE NMGFDVIRED QYSNKVPPND IISQSIAADV
EVKPTQTSIT LVVSKGKSAR PKNNTVTLKD LRNYSLKSAQ DYAKENNLTL QINQEYSDDV
EKGLVISMDP GPDTKVDKGS TVTIKVSKGP KEEKDTTITK TFTVNYVGDN LNKGEKTDNE
KENSSETSSE VSESKGDHVQ IYIKDDDHSL SNIYRDLYIK RDMSFSIPFS LKNGNGELRV
VRNGDTILNE KVTK
//
