ID D4XF92_9BURK Unreviewed; 234 AA.
AC D4XF92;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative dipeptidase E {ECO:0000313|EMBL:EFF74465.1};
DE EC=3.4.13.21 {ECO:0000313|EMBL:EFF74465.1};
GN Name=pepE {ECO:0000313|EMBL:EFF74465.1};
GN ORFNames=HMPREF0004_4139 {ECO:0000313|EMBL:EFF74465.1};
OS Achromobacter piechaudii ATCC 43553.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF74465.1, ECO:0000313|Proteomes:UP000004510};
RN [1] {ECO:0000313|Proteomes:UP000004510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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:EFF74465.1}.
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DR EMBL; ADMS01000096; EFF74465.1; -; Genomic_DNA.
DR RefSeq; WP_006220244.1; NZ_GG770409.1.
DR AlphaFoldDB; D4XF92; -.
DR MEROPS; S51.001; -.
DR PATRIC; fig|742159.3.peg.5146; -.
DR eggNOG; COG3340; Bacteria.
DR HOGENOM; CLU_071689_0_0_4; -.
DR OrthoDB; 3373764at2; -.
DR Proteomes; UP000004510; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR PANTHER; PTHR20842:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Dipeptidase {ECO:0000313|EMBL:EFF74465.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFF74465.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 234 AA; 24757 MW; 3536DF189CEC57E7 CRC64;
MNLLLLSNSS SDAGYLVHAM PDIRELIATL PPGAPAVFVP FAGVTRDWDD YTALVVSALA
DTGQSIEGLH RAQDPVAALQ NAAVIIVGGG NTFNLLGQLR RLGLLEVIAS RVRQGAAYLG
WSAGSNLTCP SICTTNDMPI TDPGGFEALG LLSFQINPHY TNAHPPGHRG ETRAQRLAEF
CTLNPAMPVL GLPEGSGLRV RGEQLALIGP HDAPLFLGRE EPRVFRPGPL EIAA
//
