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DAP_CERS4
ID   DAP_CERS4               Reviewed;         516 AA.
AC   Q3IX78;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=D-aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01960};
DE            EC=3.4.11.19 {ECO:0000255|HAMAP-Rule:MF_01960};
GN   Name=dap {ECO:0000255|HAMAP-Rule:MF_01960}; OrderedLocusNames=RHOS4_32880;
GN   ORFNames=RSP_3246;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing
CC       peptides. {ECO:0000255|HAMAP-Rule:MF_01960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal D-amino acid from a peptide, Xaa-|-
CC         Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid
CC         amides and methyl esters also are hydrolyzed, as is glycine amide.;
CC         EC=3.4.11.19; Evidence={ECO:0000255|HAMAP-Rule:MF_01960};
CC   -!- ACTIVITY REGULATION: Inhibited by beta-lactam compounds such as 6-
CC       aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and
CC       ampicillin. Inhibited by p-chloromercuribenzoate. {ECO:0000255|HAMAP-
CC       Rule:MF_01960}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01960}.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01960}.
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DR   EMBL; CP000144; ABA80856.1; -; Genomic_DNA.
DR   RefSeq; WP_011339153.1; NZ_CP030272.1.
DR   RefSeq; YP_354757.1; NC_007494.2.
DR   AlphaFoldDB; Q3IX78; -.
DR   SMR; Q3IX78; -.
DR   STRING; 272943.RSP_3246; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; ABA80856; ABA80856; RSP_3246.
DR   KEGG; rsp:RSP_3246; -.
DR   PATRIC; fig|272943.9.peg.3676; -.
DR   eggNOG; COG1680; Bacteria.
DR   OMA; RDYWAMT; -.
DR   PhylomeDB; Q3IX78; -.
DR   Proteomes; UP000002703; Chromosome 2.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.50; -; 2.
DR   Gene3D; 3.40.710.10; -; 1.
DR   HAMAP; MF_01960; D_aminopeptidase; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR027279; D_amino_pept/lipop_sf.
DR   InterPro; IPR023645; DAP.
DR   InterPro; IPR012856; DAP_B_dom.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF07930; DAP_B; 1.
DR   SUPFAM; SSF50886; SSF50886; 2.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..516
FT                   /note="D-aminopeptidase"
FT                   /id="PRO_0000250697"
FT   REGION          476..486
FT                   /note="Important for specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        64
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   BINDING         480
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
SQ   SEQUENCE   516 AA;  55379 MW;  BDA00A1D0FF7DD54 CRC64;
     MTLDLDALDR ALDALPNLFR GPGGVAGVVK DGQVVASRAW GYADLTRRRP METGTRLPIC
     SISKQFTCGA LLDTLGDTAA YDARVAEFLP QFEGPLPTLR QLCDNQSGLR DYWALTVLQG
     AEAAQTFRRE DALPLIARMK TGHFPPGTAY SYCNCNFRIV SEILESETGR ALRDLYAERI
     FGPAGMRTAE LTSDTRHPAD EVVGYEGSDA VGFFPADNGI FWIGDAGISA SLQDMLAYES
     WIDATRNDEN SIYRRISVPP AYVCGTPASY GFGLSHETVA GVKVTGHGGA LRGFRAQRFH
     AADERLSVVV IFNHEASAHA AASSLLAAAL GHEAPKGARP EGWAGQWLDP ESGLLLRVGE
     DAEGLTLRFA TGPDRLTAGE DGVPRGAGVS LAREGAMLVM NRTSDNLTVR AEPLPVVAVA
     DAGEIAGRYH ARELEADLVI EARDGGAYAG FEGLLGAGPM ERLHPVGPDV WIVTTRRSMD
     APAPGDWTLQ VRREGGAVTG LRLGCWLARR IDYARV
 
 
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