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Database: UniProt
Entry: A0A328VD95_9CHLR
LinkDB: A0A328VD95_9CHLR
Original site: A0A328VD95_9CHLR 
ID   A0A328VD95_9CHLR        Unreviewed;       278 AA.
AC   A0A328VD95;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Peptidase M55 {ECO:0000313|EMBL:RAQ94829.1};
GN   ORFNames=A4R35_04725 {ECO:0000313|EMBL:RAQ94829.1};
OS   Thermogemmatispora tikiterensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC   Thermogemmatisporaceae; Thermogemmatispora.
OX   NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ94829.1, ECO:0000313|Proteomes:UP000248706};
RN   [1] {ECO:0000313|EMBL:RAQ94829.1, ECO:0000313|Proteomes:UP000248706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T81 {ECO:0000313|EMBL:RAQ94829.1,
RC   ECO:0000313|Proteomes:UP000248706};
RA   Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA   Levin D.B.;
RT   "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT   Carbohydrate Degradation Ability.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ94829.1}.
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DR   EMBL; MCIF01000002; RAQ94829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328VD95; -.
DR   OrthoDB; 9785420at2; -.
DR   Proteomes; UP000248706; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08663; DAP_dppA_1; 1.
DR   Gene3D; 3.30.1360.130; Dipeptide transport protein; 1.
DR   Gene3D; 3.40.50.10780; Dipeptide transport protein; 1.
DR   InterPro; IPR027476; DppA_N.
DR   InterPro; IPR007035; Peptidase_M55.
DR   InterPro; IPR036177; Peptidase_M55_sf.
DR   Pfam; PF04951; Peptidase_M55; 1.
DR   PIRSF; PIRSF015853; Pep_DppA; 1.
DR   SUPFAM; SSF63992; Dipeptide transport protein; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015853-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248706};
KW   Zinc {ECO:0000256|PIRSR:PIRSR015853-2}.
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-1"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
SQ   SEQUENCE   278 AA;  30079 MW;  9D0903F418B938A0 CRC64;
     MKLFLSTDFE GTSGIVAWEQ IIEGQPEYAQ GRLLLTREVN AVITGAQEAG AREFVVNDAH
     HFMRNLHPQE LAGEATLISG RHKPLYMMEG LDSSFAGVCF VSYHGSIGAE RAVLCHTYSP
     AAIWEVRLNG QVVGEAGINA LVAAHYGVPI ILVSGDDVTV QETAIVAPAA EKIVVKHSLG
     RFAAAHLHPT RACELLRAGA QRAVERLAQG ERLEPPSFKL PVQLEVTFLV ADMAEMVCSL
     RGVERTGART VCLSGDNLLN IYRQFVAVVV LARALADR
//
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