ID A0A0F4LV32_9LACO Unreviewed; 655 AA.
AC A0A0F4LV32;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Serine-threonine protein kinase {ECO:0000313|EMBL:KJY62460.1};
GN Name=prkC {ECO:0000313|EMBL:KJY62460.1};
GN ORFNames=JG30_06750 {ECO:0000313|EMBL:KJY62460.1};
OS Bombilactobacillus mellifer.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY62460.1, ECO:0000313|Proteomes:UP000033558};
RN [1] {ECO:0000313|EMBL:KJY62460.1, ECO:0000313|Proteomes:UP000033558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin4 {ECO:0000313|EMBL:KJY62460.1,
RC ECO:0000313|Proteomes:UP000033558};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (JAN-2015) 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:KJY62460.1}.
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DR EMBL; JXJQ01000006; KJY62460.1; -; Genomic_DNA.
DR RefSeq; WP_046316182.1; NZ_KQ034028.1.
DR AlphaFoldDB; A0A0F4LV32; -.
DR STRING; 1218492.JG30_06750; -.
DR PATRIC; fig|1218492.5.peg.811; -.
DR HOGENOM; CLU_000288_135_2_9; -.
DR Proteomes; UP000033558; 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 GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd06577; PASTA_pknB; 2.
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 Pfam; PF21160; PrkC-like_PASTA-like; 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}; Kinase {ECO:0000313|EMBL:KJY62460.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000033558};
KW Transferase {ECO:0000313|EMBL:KJY62460.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..272
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 347..414
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 415..478
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 479..547
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 548..579
FT /note="Disordered"
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 655 AA; 72468 MW; 0F8AE922D1EE0673 CRC64;
MINKGDLIAD RYLILDTLGE GGMSNVYLAE DQFLHRKVAL KSLRFDVQNN PQIKIRFKRE
SIAMSELSSP YIVNILDVGD DDSFPYIVME YVAGSTLKQY IHQHYPLEYP LVVRFMMEIL
QGVTVAHRHG IIHRDLKPQN VMITPSNHVK VSDFGIALSL GEQSITQTDS TLGSVHYMAP
ERVRGERATA QSDIYSLGII LYEMLTGKLP FDGETSLAIA LKHFNEEIPD MKKALPDLPQ
PLENVVLKAT AKDPKQRYSS TQAMANDLRT ALDPNRAQEP KFVALPVKTG SNLEATKVMP
NLSKNDAPKT QATPPKPRRR WWRKKRWWLF GLLLLGLILL GGWLFWGRAE VAVPDVNNLS
LSQANNRLVA AKLKPGAVIK QTSATVPAKK VIRTIPNHGV RLKTGAKVKL VISSGSKKQR
VPNVVGLNYA AAAAKLRGQG YQVQRVNRYS KNVSSGIVLR QSPKYAHARQ KVRLVVSLGP
HRHNLTVKDL TGYSLRSARD YADEVGLTLV VKEQASDSVD KGLIISQDPS PGTRVTPGSD
LTVVVSTGAA NNKNSNDKTS DNDAANNDHG ANTNTPQNYE KTVTIPYDSQ NATGSNQVQI
YLKDNNRNLT DLYKAMTIKA DTNVVLPFVL KKGDTGQYRI VRDGQVIESQ TVTGN
//
