ID D9VVK5_9ACTN Unreviewed; 418 AA.
AC D9VVK5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Metal-dependent amidase/aminoacylase/carboxypeptidase {ECO:0000313|EMBL:EFL17121.1};
GN ORFNames=SSNG_04373 {ECO:0000313|EMBL:EFL17121.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL17121.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL17121.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL17121.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657750; EFL17121.1; -; Genomic_DNA.
DR RefSeq; WP_007266050.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VVK5; -.
DR STRING; 253839.SSNG_04373; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:EFL17121.1};
KW Hydrolase {ECO:0000313|EMBL:EFL17121.1};
KW Protease {ECO:0000313|EMBL:EFL17121.1}.
FT DOMAIN 207..299
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 44982 MW; 8F3B49A25E8A2739 CRC64;
MSREPQTALP GKPVRPELPG KLPDRLRAEL IAFRRDLHMH PELGNQEFRT TAAIKARLEK
AGLRPRVLKS GTGLICDVGT WDGGRPMLAL RADIDALPIP DAKTHVSYRS TYPDRAHACG
HDVHTTVVLG AGLVLAELDR QGLLPRPVRL LFQPAEEVLP GGATEAIESG VLDGVGKIIA
VHCDPRVDAG MIGLRPGPIT SACDRLEVTL GGPGGHTARP HLTTDMVTAA ARVAIDVPAL
LARRMDARSG MSVTWGRIES GHACNVVPMH AELSGTVRCL DLNAWYEAPD MIHAAIDEVA
TMHGAKFEIN HVRGVPPVVN DPVVTELLRE AMGARRGPES VEDTEQSLGG EDFSWYLEHV
PGAMARLGVR RPGDTAKRDL HRGDFDVDES SIGYGVEFFT AAALLDGRRN SPVTSKIG
//
