GenomeNet

Database: UniProt
Entry: E8X553_GRATM
LinkDB: E8X553_GRATM
Original site: E8X553_GRATM 
ID   E8X553_GRATM            Unreviewed;       730 AA.
AC   E8X553;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Glutamate carboxypeptidase II {ECO:0000313|EMBL:ADW68317.1};
DE            EC=3.4.17.21 {ECO:0000313|EMBL:ADW68317.1};
GN   OrderedLocusNames=AciX9_1255 {ECO:0000313|EMBL:ADW68317.1};
OS   Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN   [1] {ECO:0000313|Proteomes:UP000000343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA   Haggblom M.M., Woyke T.;
RT   "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002480; ADW68317.1; -; Genomic_DNA.
DR   RefSeq; WP_013579640.1; NC_015064.1.
DR   AlphaFoldDB; E8X553; -.
DR   STRING; 1198114.AciX9_1255; -.
DR   PaxDb; 1198114-AciX9_1255; -.
DR   KEGG; acm:AciX9_1255; -.
DR   eggNOG; COG2234; Bacteria.
DR   HOGENOM; CLU_005688_2_1_0; -.
DR   OrthoDB; 233977at2; -.
DR   Proteomes; UP000000343; Chromosome.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR   CDD; cd08022; M28_PSMA_like; 1.
DR   CDD; cd02121; PA_GCPII_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR039373; Peptidase_M28B.
DR   InterPro; IPR007365; TFR-like_dimer_dom.
DR   InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR   PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR   PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   Pfam; PF04253; TFR_dimer; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:ADW68317.1};
KW   Hydrolase {ECO:0000313|EMBL:ADW68317.1};
KW   Protease {ECO:0000313|EMBL:ADW68317.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000343};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..730
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003234387"
FT   DOMAIN          164..248
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          348..559
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          623..725
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          125..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  77980 MW;  BAA8C03B77E1DE8E CRC64;
     MNRPAILPVL LALSSAAALA QSATQSSVPP APTSVFGYKD FSQQAKWDAA FQAIPDSKLA
     GEHLKTLTKA PHWASSPEDY ATAEYVAAKF KAAGLQTEIV PYKVLLNKPV KIVIEAFDAT
     GAKLMSGPSP EHVDPTKDGG DPFQDDPRIL PAFNGSSPSA DIAAEVVYAN YGTPADFKKL
     ADLGVDVKGK IVIVRYGANY RGIKVYDAQK AGAAGVLIFS DPEDDGYFRG DKYPKGPYRP
     DSAVQRGAVQ FLPIYPGDAT TPGIASTPNL PDSQRIPADK IQANWPSIPS NPLSYKDAAP
     ILEALGGPAA PHAWQGALPF AYHVGGGPKI MVHMHLEQDT KLRTIWDVIG TIPGTDPAEK
     NDWVVAGNHR DAWVYGAVDP NSGTAAMLET VHGLGDLLKQ GWKPKRTIVI GSWDAEEEGL
     IGSTEWVEAH PTQLRNAVAY FNTDVGVSGP NFNASAVPSL KQFVREVTRE VPSPAGGTVY
     DQWLKGQTDR RNESEDEGGA TRGARPAGRN GGTAGEIRIG DLGSGSDYTP FLQHQGVPAT
     DIGSGGPYGV YHSVFDNYNW FIKNADPTFV YEQQQARVFG LEILHMADAD VLPYDYQAYG
     TQLKGYIEAA KSRSSAMGLD FAALESAANR FAAAGVVIRQ RQLTPSNTAT LNTALRSAED
     ALLDPAGLPH RAWYKHTIYA PGEFTGYAAV VIPGVNEGID AIDKARTQTQ IESLTAAVNR
     SAAILEAAAK
//
DBGET integrated database retrieval system