ID A5N891_CLOK5 Unreviewed; 390 AA.
AC A5N891;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Predicted amidohydrolase {ECO:0000313|EMBL:EDK33522.1};
GN OrderedLocusNames=CKL_1480 {ECO:0000313|EMBL:EDK33522.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33522.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK33522.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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DR EMBL; CP000673; EDK33522.1; -; Genomic_DNA.
DR RefSeq; WP_012101872.1; NC_009706.1.
DR AlphaFoldDB; A5N891; -.
DR STRING; 431943.CKL_1480; -.
DR KEGG; ckl:CKL_1480; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR Proteomes; UP000002411; Chromosome.
DR GO; GO:0016787; F:hydrolase 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 Hydrolase {ECO:0000313|EMBL:EDK33522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT DOMAIN 187..276
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 390 AA; 43252 MW; 8B0DCC5E036A50E3 CRC64;
MARDFFNMAQ SIKKELIDIR RDLHRHPELG YEEERTSFKI KEFLKKIGIE YMETAGTGVC
GIIRGKGNKT IGIRADIDAL PLEDHKNCSY SSKVKGKMHA CGHDAHTTIL LGTAKVLNSV
KDELKGTVKL FFEPAEETTG GAKLMVKEGA LENPRVDRVI GLHVDENIEV GNIGVKLGVV
NAASNPFTIK IKGVGAHGAR PHMGVDPIVI SSHVILALQQ IVSRELPPTD AAVITVGSIH
GGTAQNIIPE EVVIAGTMRT MRTEHREYVK ERLREITFGV VNSMRGKYEI DIEESYPCLY
NDDDVIKDIL KAAYKEIGEE HVKMLESPSM GVESFAYFSM ERPSAFYYLG CRNESKNIIY
PAHGSLFDID EDCLPIGVSI QCRAAYDFLK
//
