ID A0A147KCR5_9BACI Unreviewed; 397 AA.
AC A0A147KCR5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=Q75_00725 {ECO:0000313|EMBL:KUP09475.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP09475.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP09475.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|PIRNR:PIRNR037226}.
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:KUP09475.1}.
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DR EMBL; LDYG01000001; KUP09475.1; -; Genomic_DNA.
DR RefSeq; WP_059350001.1; NZ_LDYG01000001.1.
DR AlphaFoldDB; A0A147KCR5; -.
DR STRING; 1150625.Q75_00725; -.
DR PATRIC; fig|1150625.3.peg.150; -.
DR OrthoDB; 9781032at2; -.
DR Proteomes; UP000074108; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR CDD; cd03887; M20_Acy1L2; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KUP09475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000074108}.
FT DOMAIN 181..269
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 397 AA; 42411 MW; 2E90C0FC69C907D8 CRC64;
MLASTIIQLE SAIFTSIENN QALYIETSHK IHQHPEIGNE EVFASELLTS ILEEAGFGIQ
RDILKHPTGF IARKKSTKPG ASIGFLAEYD ALPGLGHACG HNIIGTTSVA AAIAIGELID
QVGGEVVVFG TPAEEGGPNG SAKATFVQHG LVQDLDACMM VHPLGVTSGT APSLAVDPVD
FEFFGKPAHA AANPEAGINA LDGVIQLYNG INALRQHVTS DVKIHGIILD GGQAPNIVPD
YARARFFIRA AHRSTCDQIT KRVFQIAEGA ALSCGATMKM TRIQNGVDHF HRTPKFDGVF
RKRIEQLGEE YQDREQGIGS TDAGNVSQVI PTIHPYIKIG PSSLVAHTVE FREAAASPKG
DAALLKGAKA LALTALDLFT NQELLEDIKK EHQAHLE
//
