(data stored in ACNUC7421 zone)

SWISSPROT: PEPQ_SHESH

ID   PEPQ_SHESH              Reviewed;         439 AA.
AC   A8FP64;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 72.
DE   RecName: Full=Xaa-Pro dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            Short=X-Pro dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            EC=3.4.13.9 {ECO:0000255|HAMAP-Rule:MF_01279};
DE   AltName: Full=Imidodipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE   AltName: Full=Proline dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            Short=Prolidase {ECO:0000255|HAMAP-Rule:MF_01279};
GN   Name=pepQ {ECO:0000255|HAMAP-Rule:MF_01279};
GN   OrderedLocusNames=Ssed_0024;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-
CC       terminal position. {ECO:0000255|HAMAP-Rule:MF_01279}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Xaa-|-Pro dipeptides; also acts
CC       on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
CC       {ECO:0000255|HAMAP-Rule:MF_01279}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01279};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01279};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type
CC       prolidase subfamily. {ECO:0000255|HAMAP-Rule:MF_01279}.
DR   EMBL; CP000821; ABV34637.1; -; Genomic_DNA.
DR   RefSeq; WP_012004163.1; NC_009831.1.
DR   ProteinModelPortal; A8FP64; -.
DR   SMR; A8FP64; -.
DR   STRING; 425104.Ssed_0024; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; ABV34637; ABV34637; Ssed_0024.
DR   KEGG; sse:Ssed_0024; -.
DR   eggNOG; ENOG4105D9Y; Bacteria.
DR   eggNOG; COG0006; LUCA.
DR   HOGENOM; HOG000290531; -.
DR   KO; K01271; -.
DR   OMA; MQDDTGT; -.
DR   OrthoDB; POG091H0HZN; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016795; F:phosphoric triester hydrolase activity; IEA:InterPro.
DR   GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR   HAMAP; MF_01279; X_Pro_dipeptid; 1.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   InterPro; IPR022846; X_Pro_dipept.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FP64.
DR   SWISS-2DPAGE; A8FP64.
KW   Complete proteome; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW   Metalloprotease; Protease.
FT   CHAIN         1    439       Xaa-Pro dipeptidase.
FT                                /FTId=PRO_1000085889.
FT   METAL       244    244       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       255    255       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       255    255       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       335    335       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       380    380       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       419    419       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       419    419       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
SQ   SEQUENCE   439 AA;  50059 MW;  E52F858A4A581E74 CRC64;
     MDQLTNHFHA HVAELNRRVA EIVARENLSG LVIHSGQPHR QFLDDMDYPF KVNPHFKAWL
     PILDNPHCWL LVNGRDKPQL IFYRPVDFWH KVADLPDEFW TAHVDIKLLT KADKVADLLP
     KDIVDWAYVG EHLDVAEVLG FKTRNPDAVM SYLHYHRATK TEYELACMRK SNEIAVKGHV
     AAKNAFYNGG SEFEIQQQYL MATNQGENEV PYGNIIALNR NASILHYTKL ENQSPQPRRS
     FLIDAGANFF GYASDITRTY AFEKNIFSEL IEAMDRAQLE IIDTMRPGVK YVDLHLATHQ
     KVAQMLIDFD LATGDREGLI EQGITSVFFP HGLGHMLGLQ VHDMGGFLHD ERGTHIAAPD
     AHPFLRCTRT LAANQVLTIE PGLYIIDSLL QGLKQDNRQH QVNWNSVDLL RPFGGIRIED
     NVIVHSDKNE NMTRDLGLD
//

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