ID N2INX4_9PSED Unreviewed; 416 AA.
AC N2INX4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=HMPREF1487_08526 {ECO:0000313|EMBL:ENA29107.1};
OS Pseudomonas sp. HPB0071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA29107.1, ECO:0000313|Proteomes:UP000017050};
RN [1] {ECO:0000313|EMBL:ENA29107.1, ECO:0000313|Proteomes:UP000017050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPB0071 {ECO:0000313|EMBL:ENA29107.1,
RC ECO:0000313|Proteomes:UP000017050};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J., Dai D.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Pseudomonas sp. HPB0071.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:ENA29107.1}.
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DR EMBL; AQFP01000015; ENA29107.1; -; Genomic_DNA.
DR RefSeq; WP_010798684.1; NZ_KI517368.1.
DR AlphaFoldDB; N2INX4; -.
DR PATRIC; fig|1203578.3.peg.4242; -.
DR HOGENOM; CLU_021802_7_2_6; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000017050; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd03885; M20_CPDG2; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF10; BLL3749 PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000017050};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..416
FT /note="Peptidase M20 dimerisation domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004115683"
FT DOMAIN 214..311
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 416 AA; 44396 MW; 660482E1F4943EC9 CRC64;
MTVMLRRATC SLSLAIAFAF STASTVQAEP NHPVQSHAEQ YKEEALKLLE QLVNIDSGSG
YAPGLIQVGQ IAADQLKQLG ATIETVPNSP PDKSHHIVAT LKGTGKAKIL LMAHMDTVFK
EGSAKERPFH IKDGRAYGPG VMDDKGGIVA GIYALKILKD LNFKDYAQIT FLLDASEETG
SDAATQLIQR VAREHDVTLN LEPGRPADGL VAWRKGSATA TVDVTGKAAH AGVAPELGRN
AAMEISHQVL QLGKLGDVEK KTTVNFTVID AGDRTNVIPD SATAKADVRV AVPEEFDRVE
QDMARVSANK LIQETDVKTH LHRGLPPMPQ TAETDRLVSM AQNIYGEIGR KLTIEGSGGA
ADASLAAGVG VPTLDGFGIV GGNIHTPEEY AEVESVAPRL YLLARMIMEL AQRDKG
//
