ID A0A136LSK2_9BACT Unreviewed; 692 AA.
AC A0A136LSK2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate carboxypeptidase II {ECO:0000313|EMBL:KXK24640.1};
GN ORFNames=UZ12_BCD005001921 {ECO:0000313|EMBL:KXK24640.1};
OS Bacteroidetes bacterium OLB12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK24640.1, ECO:0000313|Proteomes:UP000070129};
RN [1] {ECO:0000313|EMBL:KXK24640.1, ECO:0000313|Proteomes:UP000070129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK24640.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK24640.1}.
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DR EMBL; LNFR01000070; KXK24640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LSK2; -.
DR STRING; 1619897.UZ12_BCD005001921; -.
DR PATRIC; fig|1619897.3.peg.2096; -.
DR Proteomes; UP000070129; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:KXK24640.1};
KW Hydrolase {ECO:0000313|EMBL:KXK24640.1};
KW Protease {ECO:0000313|EMBL:KXK24640.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..692
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007475214"
FT DOMAIN 142..203
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 327..510
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 578..684
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 692 AA; 76477 MW; B6F0B5919DBA3C23 CRC64;
MKTLLALLLL SIPAFSQTYY GFSSNSSATQ SKAEEVFLQQ QQNERYKNHL KELTKEPHIA
GSKANERVRD YLAEVMRKAG FQVEIFPYDI YLPVMPGTAY AEVVEPIRIP LNNKEYIHHE
DPYTTNPNLP VGFNAYSGSG DVTAEVVYAN YGRREDFQKL EALGVSVKGK IVLARYGGNF
RGYKAKYAQA YGAAGLIIFT DPGDSGYTKG LVYPDGPYSN ESSIQRGSLL TADWTGDPLT
PFEPALPLDG KKKVVRKKPE EVSGMHAIPV LPLPYGSAKE IFARMKGKVV PAGWQGGLPY
TYRLEGGSEL KVRVSVQQER KIQRVYNVVG TLVGSESPNE WIIAGSHYDA WGHGATDPNS
GTAMLLSLSE SLGKLSQAGY KPKRTIKIAH WDAEEQGVIG STEWVEQFRD ELNAKGVAYF
NADGAVSGRN FGGASSPSLK ALFIESTKVI PYPDSAKSVY DHWRKQNPNP PIGNLGGGSD
HIAFYTHVGI PSWSGGTGGP TMYHSNHDTF YFYEHFSDPT FSMGPLVERV FGIAALRLAN
ADVLPYNVSR YGADLRMHFE GIQKAINAYD KSENKFSFET LLKASDELKK IGEDCETALK
NANAAKLKTI NAELLLLERQ WLDPEGMPFG NWYKSLYASP DPYSGYASAI LPGFQYEVAN
KSTANLKMWE QKYLAAIARL KSKLETITKL AQ
//
