ID K4LS04_THEPS Unreviewed; 138 AA.
AC K4LS04;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Ribonuclease VapC {ECO:0000256|HAMAP-Rule:MF_00265};
DE Short=RNase VapC {ECO:0000256|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC {ECO:0000256|HAMAP-Rule:MF_00265};
GN Name=vapC {ECO:0000256|HAMAP-Rule:MF_00265};
GN OrderedLocusNames=Tph_c06220 {ECO:0000313|EMBL:AFV10859.1};
OS Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermacetogenium.
OX NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV10859.1, ECO:0000313|Proteomes:UP000000467};
RN [1] {ECO:0000313|EMBL:AFV10859.1, ECO:0000313|Proteomes:UP000000467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC {ECO:0000313|Proteomes:UP000000467};
RX PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA Schink B.;
RT "Genome-guided analysis of physiological and morphological traits of the
RT fermentative acetate oxidizer Thermacetogenium phaeum.";
RL BMC Genomics 13:723-723(2012).
CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) system. An RNase.
CC {ECO:0000256|HAMAP-Rule:MF_00265}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00265};
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000256|ARBA:ARBA00038093, ECO:0000256|HAMAP-Rule:MF_00265}.
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DR EMBL; CP003732; AFV10859.1; -; Genomic_DNA.
DR RefSeq; WP_015049777.1; NZ_KI912609.1.
DR AlphaFoldDB; K4LS04; -.
DR STRING; 1089553.Tph_c06220; -.
DR KEGG; tpz:Tph_c06220; -.
DR eggNOG; COG1848; Bacteria.
DR HOGENOM; CLU_135601_1_2_9; -.
DR OrthoDB; 1723839at2; -.
DR Proteomes; UP000000467; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd18689; PIN_VapC-like; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR022907; VapC_family.
DR PANTHER; PTHR33653; RIBONUCLEASE VAPC2; 1.
DR PANTHER; PTHR33653:SF1; RIBONUCLEASE VAPC2; 1.
DR Pfam; PF01850; PIN; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00265};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00265};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00265};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00265};
KW Reference proteome {ECO:0000313|Proteomes:UP000000467};
KW Toxin {ECO:0000256|HAMAP-Rule:MF_00265};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649, ECO:0000256|HAMAP-
KW Rule:MF_00265}.
FT DOMAIN 5..123
FT /note="PIN"
FT /evidence="ECO:0000259|Pfam:PF01850"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ SEQUENCE 138 AA; 15579 MW; 1403C565A8AF57EA CRC64;
MSDYYVLDAC ALIAFLNDEA GADVVEELLR KSNRQEPNLF LHRLNLLEVY YGIYREVGPE
TSEQVLGKIR ALPVTEVTEI TQEVFLEAGR LKATYRLSLA DSIAAAEAKV RGASLVTADH
HEFNLIATRE DIAFHWIR
//