ID A6TPW1_ALKMQ Unreviewed; 273 AA.
AC A6TPW1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Peptidase M55, D-aminopeptidase {ECO:0000313|EMBL:ABR48229.1};
GN OrderedLocusNames=Amet_2068 {ECO:0000313|EMBL:ABR48229.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR48229.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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DR EMBL; CP000724; ABR48229.1; -; Genomic_DNA.
DR RefSeq; WP_012063209.1; NC_009633.1.
DR AlphaFoldDB; A6TPW1; -.
DR STRING; 293826.Amet_2068; -.
DR KEGG; amt:Amet_2068; -.
DR eggNOG; COG2362; Bacteria.
DR HOGENOM; CLU_086038_1_0_9; -.
DR OrthoDB; 9785420at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08769; DAP_dppA_2; 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 Aminopeptidase {ECO:0000313|EMBL:ABR48229.1};
KW Hydrolase {ECO:0000313|EMBL:ABR48229.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015853-2};
KW Protease {ECO:0000313|EMBL:ABR48229.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572};
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 273 AA; 29997 MW; D9A0FD2C0121A6C8 CRC64;
MKIYVSADIE GIWGVVSPRQ IGGESEDYTR ARKLMTQEVN LLCQYLLQNG ASEIVINDSH
GPMDNIIIEE LNPEVSLISG YPKDLSMMEG IDESFDCVML IGYHPKAGTE KGIFDHTYAG
RVIRNLYIDE EELGEVGLNA LVAGGFGVPV VLVSGDEKVT QDVKMEIGDI ETVAVKKALS
RYCAKNISFL KLEKLYSEAV KNALKDVKKY PIKKPSSSPV LKLELYQAVM AETVACIPGV
KKVGPTSVEY IAEEMADVYK ALRSIVTVAQ NLI
//
