ID A0A024QFB9_9BACI Unreviewed; 149 AA.
AC A0A024QFB9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Protein SprT-like {ECO:0000256|HAMAP-Rule:MF_00745};
GN ORFNames=BN990_03243 {ECO:0000313|EMBL:CDQ40895.1};
OS Virgibacillus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ40895.1, ECO:0000313|Proteomes:UP000028875};
RN [1] {ECO:0000313|EMBL:CDQ40895.1, ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ40895.1,
RC ECO:0000313|Proteomes:UP000028875};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00745};
CC Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00745};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00745}.
CC -!- SIMILARITY: Belongs to the SprT family. {ECO:0000256|HAMAP-
CC Rule:MF_00745}.
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:CDQ40895.1}.
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DR EMBL; CCDP010000002; CDQ40895.1; -; Genomic_DNA.
DR RefSeq; WP_021288577.1; NZ_WMER01000009.1.
DR AlphaFoldDB; A0A024QFB9; -.
DR STRING; 1462526.BN990_03243; -.
DR eggNOG; COG3091; Bacteria.
DR OrthoDB; 9799909at2; -.
DR Proteomes; UP000028875; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR HAMAP; MF_00745; SprT_like; 1.
DR InterPro; IPR006640; SprT-like_domain.
DR InterPro; IPR035240; SprT_Zn_ribbon.
DR InterPro; IPR023524; Uncharacterised_SprT-like.
DR Pfam; PF10263; SprT-like; 1.
DR Pfam; PF17283; Zn_ribbon_SprT; 1.
DR SMART; SM00731; SprT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00745};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00745};
KW Reference proteome {ECO:0000313|Proteomes:UP000028875};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00745}.
FT DOMAIN 7..149
FT /note="SprT-like"
FT /evidence="ECO:0000259|SMART:SM00731"
FT ACT_SITE 71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00745"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00745"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00745"
SQ SEQUENCE 149 AA; 17848 MW; E89E519CEF22343B CRC64;
MRLPDDNELF ELVDRLSIVH FNKPFLHKVS FNSRLRTTGG RYIPGRKTIE LNPKYAMERD
ETEFIGIIKH ELCHYHLHIE GKGYKHGDRE FKELLKATGS PRHCKPLPSQ MKYNYEYQCR
NCNQTYRRMR RINTSKYRCG KCKGRIILQ
//
