ID G4D308_9FIRM Unreviewed; 398 AA.
AC G4D308;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=M20D family peptidase {ECO:0000313|EMBL:EGY80089.1};
DE EC=3.4.17.- {ECO:0000313|EMBL:EGY80089.1};
GN ORFNames=HMPREF9129_0788 {ECO:0000313|EMBL:EGY80089.1};
OS Peptoniphilus indolicus ATCC 29427.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=997350 {ECO:0000313|EMBL:EGY80089.1, ECO:0000313|Proteomes:UP000003422};
RN [1] {ECO:0000313|EMBL:EGY80089.1, ECO:0000313|Proteomes:UP000003422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29427 {ECO:0000313|EMBL:EGY80089.1,
RC ECO:0000313|Proteomes:UP000003422};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGY80089.1}.
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DR EMBL; AGBB01000068; EGY80089.1; -; Genomic_DNA.
DR AlphaFoldDB; G4D308; -.
DR STRING; 997350.HMPREF9129_0788; -.
DR PATRIC; fig|997350.3.peg.760; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR Proteomes; UP000003422; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd03886; M20_Acy1; 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 NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:EGY80089.1};
KW Hydrolase {ECO:0000313|EMBL:EGY80089.1};
KW Protease {ECO:0000313|EMBL:EGY80089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003422}.
FT DOMAIN 193..287
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 398 AA; 43785 MW; AFA6F6C9BB5EF65A CRC64;
MINVNYIEFG EKISDHLRSL RAELHSNPEP STFEEITSQI ILKELKNIGI TDIQTGLGNG
KHGIIANIAG GLPGKKVALR ADMDALAIEE ETDLECTSKN KGYMHACGHD NHVAMVLGAA
NIIYQNKDKL KGSVRLIFQP AEELSPEGGA KSMILEGALK DVDAIFGFHV WPELPFGVMG
FKEGPLMAAS DHFYVNIKGK ASHAAGPENG VDAIVAGCEY VGAIQHIVSR NISAIDNVVI
TVGTINAGTR YNIVAEDFKV EGTCRTLSPE IRDLVENRLK EILEGICKVY GCKGELDYQR
GYIPLINDSE MTKYAKKVAL DLFGEKYVQD VKEPVLKAED FGFYLAEKPG SFIWLGTAEQ
DKDYWPLHNS HFSPNDEVLY RGSAMLAKLA FEFTESNK
//
