ID   A0A1J6W5S8_9BACI        Unreviewed;       155 AA.
AC   A0A1J6W5S8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Protein SprT-like {ECO:0000256|HAMAP-Rule:MF_00745};
GN   ORFNames=BHE18_00255 {ECO:0000313|EMBL:OIU72981.1};
OS   Rossellomorea aquimaris.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU72981.1, ECO:0000313|Proteomes:UP000182062};
RN   [1] {ECO:0000313|EMBL:OIU72981.1, ECO:0000313|Proteomes:UP000182062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAMM {ECO:0000313|EMBL:OIU72981.1,
RC   ECO:0000313|Proteomes:UP000182062};
RA   Waghmode S.R., Suryavanshi M.V.;
RT   "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT   biosurfactant production capacities.";
RL   Submitted (SEP-2016) 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:OIU72981.1}.
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DR   EMBL; MINN01000044; OIU72981.1; -; Genomic_DNA.
DR   RefSeq; WP_071616984.1; NZ_MINN01000044.1.
DR   AlphaFoldDB; A0A1J6W5S8; -.
DR   OrthoDB; 9799909at2; -.
DR   Proteomes; UP000182062; 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:UP000182062};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00745}.
FT   DOMAIN          4..148
FT                   /note="SprT-like"
FT                   /evidence="ECO:0000259|SMART:SM00731"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00745"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00745"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00745"
SQ   SEQUENCE   155 AA;  18444 MW;  CC379888281D1BA9 CRC64;
     MTNQELQSLV EEISIRHFQK PFRHKAYFNT RLRTTGGRYM LGSHNIDING KYLEEHGLPE
     LIGIIKHELC HYHLHIEGKG YKHRDPEFKF LLEQVGGARH CTPLQKTKKN RRILIYSCSK
     CNLMFKRRRR IDTKKYVCGK CKGKLVFKEE LMQEL
//