ID   A0A1F5AR95_9BACT        Unreviewed;       713 AA.
AC   A0A1F5AR95;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glutamate carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2Y69_10540 {ECO:0000313|EMBL:OGD20594.1};
OS   Candidatus Aminicenantes bacterium RBG_13_59_9.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1797268 {ECO:0000313|EMBL:OGD20594.1, ECO:0000313|Proteomes:UP000177868};
RN   [1] {ECO:0000313|EMBL:OGD20594.1, ECO:0000313|Proteomes:UP000177868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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:OGD20594.1}.
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DR   EMBL; MEXW01000150; OGD20594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5AR95; -.
DR   Proteomes; UP000177868; Unassembled WGS sequence.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
FT   DOMAIN          160..235
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          344..531
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          597..705
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
SQ   SEQUENCE   713 AA;  79353 MW;  ADA526F5A8F38F22 CRC64;
     MKSRLVLPIS GQLTIAALFV FSACGSPPPR EPVKLSGYLN SSVDAQLESE KLILSVPSSL
     QFGAHLLYLT EEPHQTGSPR NYELADYVRD RFLEYGLEDV HFHDTPALIG YGRSLLVEIT
     GPQKKKLKLA EDSYPPDKDS GLYSDGSVVP YHEYALSGDV TTEVVYANGG SPEDFAELDR
     LGIDVKGKIV ILRYSNPYSY RGYKVYLAES RGAAAAIIYS DPQDDGFFRG EVYPHGPWGP
     PSHIQWGGIV YDWFGFGITP FTFHWKKQED GTWVEGPVRD RLLPKIPSVP MSHEDASEIL
     RLLGGPAVPE GWQGGLPFTY HVGPGPVKVH MKVDNFEKIA PMRNVMAMVR GSHDPDKWVV
     AGNHRDAWIY GGYDPSSGTA ALLEVARALG TAVKQGFRPS RTIVLANWDA EEDLLGGSTS
     WAKEKRAKLL RDGVVYVNLD SAACGPEFNG GSTPALAEFL RGTAKAVPHP DIPGGSVHDH
     WLKASKSGKA EVDAIVGATD YTAFQENIGM SCIDMTFGES YGVYHSMYDN YFWMSEIGDP
     GFRYNVTCSQ MLAVIIWRLA NADILPLEYS SYAKAALDAI EEVEHMALPQ RKIDLGRAKK
     AARRWLEAAS AWENNVRRFL SAEKSLDSKR ASEINSLLLE VERAMTEEEG LKSRPYFKHL
     IYAPQPTYRT ELLPRIFEAI QAQEWDDIPR YEEQLVKAFD RAGRLMREAS RLL
//