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Database: UniProt
Entry: A0A553H2L2_9PSED
LinkDB: A0A553H2L2_9PSED
Original site: A0A553H2L2_9PSED 
ID   A0A553H2L2_9PSED        Unreviewed;       164 AA.
AC   A0A553H2L2;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein SprT {ECO:0000256|ARBA:ARBA00020082, ECO:0000256|HAMAP-Rule:MF_00746};
GN   Name=sprT {ECO:0000256|HAMAP-Rule:MF_00746};
GN   ORFNames=FM069_06070 {ECO:0000313|EMBL:TRX75997.1};
OS   Pseudomonas mangiferae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2593654 {ECO:0000313|EMBL:TRX75997.1, ECO:0000313|Proteomes:UP000315235};
RN   [1] {ECO:0000313|EMBL:TRX75997.1, ECO:0000313|Proteomes:UP000315235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMKU_BBB3-04 {ECO:0000313|EMBL:TRX75997.1,
RC   ECO:0000313|Proteomes:UP000315235};
RA   Srisuk N., Anurat P.;
RT   "Pseudomonas mangiferae sp. nov., isolated from bark of mango tree in
RT   Thailand.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00746};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00746};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00746}.
CC   -!- SIMILARITY: Belongs to the SprT family. {ECO:0000256|ARBA:ARBA00006591,
CC       ECO:0000256|HAMAP-Rule:MF_00746}.
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:TRX75997.1}.
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DR   EMBL; VJOY01000003; TRX75997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A553H2L2; -.
DR   OrthoDB; 267364at2; -.
DR   Proteomes; UP000315235; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00746; SprT; 1.
DR   InterPro; IPR006640; SprT-like_domain.
DR   InterPro; IPR035240; SprT_Zn_ribbon.
DR   InterPro; IPR023483; Uncharacterised_SprT.
DR   PANTHER; PTHR38773; PROTEIN SPRT; 1.
DR   PANTHER; PTHR38773:SF1; PROTEIN SPRT; 1.
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_00746};
KW   Hydrolase {ECO:0000313|EMBL:TRX75997.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00746};
KW   Metalloprotease {ECO:0000313|EMBL:TRX75997.1};
KW   Protease {ECO:0000313|EMBL:TRX75997.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000315235};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00746}.
FT   DOMAIN          7..158
FT                   /note="SprT-like"
FT                   /evidence="ECO:0000259|SMART:SM00731"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00746"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00746"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00746"
SQ   SEQUENCE   164 AA;  19464 MW;  13A8DA779DB800F0 CRC64;
     MPDRLLAKVE ACYQQAEAFF HRRFTRPDVS FKLRGQKAGV AHLQENRLRF NPQLYRDNQD
     DFLRQTVPHE VAHLIAHQVF GGRIQPHGEE WQLIMRGVYE LQPHRCHSYA VERRQGTRYI
     YRCGCPDQDF PFTAQRHALV GRGRRYICRR CRGPLTFTGE QRVE
//
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