(data stored in ACNUC7421 zone)

SWISSPROT: B4SHK6_STRM5

ID   B4SHK6_STRM5            Unreviewed;       237 AA.
AC   B4SHK6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=D-alanyl-D-alanine dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE            Short=D-Ala-D-Ala dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE            EC=3.4.13.22 {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE   Flags: Precursor;
GN   Name=ddpX {ECO:0000256|HAMAP-Rule:MF_01924};
GN   OrderedLocusNames=Smal_0344 {ECO:0000313|EMBL:ACF50049.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50049.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50049.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50049.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine
CC       dipeptide. {ECO:0000256|HAMAP-Rule:MF_01924,
CC       ECO:0000256|PIRNR:PIRNR026671}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine;
CC         Xref=Rhea:RHEA:20661, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822; EC=3.4.13.22; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01924};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01924};
CC   -!- SIMILARITY: Belongs to the peptidase M15D family.
CC       {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671}.
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DR   EMBL; CP001111; ACF50049.1; -; Genomic_DNA.
DR   RefSeq; WP_012509860.1; NC_011071.1.
DR   STRING; 391008.Smal_0344; -.
DR   MEROPS; M15.011; -.
DR   EnsemblBacteria; ACF50049; ACF50049; Smal_0344.
DR   KEGG; smt:Smal_0344; -.
DR   eggNOG; ENOG4108UQS; Bacteria.
DR   eggNOG; COG2173; LUCA.
DR   HOGENOM; HOG000200848; -.
DR   KO; K08641; -.
DR   OMA; IRTEWWH; -.
DR   OrthoDB; 880710at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01795-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   HAMAP; MF_01924; A_A_dipeptidase; 1.
DR   InterPro; IPR000755; A_A_dipeptidase.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   Pfam; PF01427; Peptidase_M15; 1.
DR   PIRSF; PIRSF026671; AA_dipeptidase; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SHK6.
DR   SWISS-2DPAGE; B4SHK6.
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR026671};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    237       D-alanyl-D-alanine dipeptidase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002822913.
FT   ACT_SITE    216    216       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       149    149       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       156    156       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01924}.
FT   METAL       219    219       Zinc; via pros nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   SITE        104    104       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
SQ   SEQUENCE   237 AA;  25927 MW;  8058B4CF561E1584 CRC64;
     MTSRICISLV LATALAATTR AAEPPRVSPA TDAASAGLVE IRTLSPGIDM DIRYAGANNF
     TGARVPGYEA PSCYLLAPVA KALAQVEQDL RADGFGLRIY DCYRPVRSVQ AFMAWVNDPS
     ELSRKALQYP DLDKPRLLAD GYIAERSGHS RGATVDLGLL DCRNGRCKPM DMGTDFDFFG
     PRAHTQTSGL SDAQQANRQQ LVSAMARRGF ANYPKEWWHY TLQPEPDPGT AYDVPVR
//

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