ID   Y3995_MYCS2             Reviewed;         438 AA.
AC   A0QZE3; I7GB47;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Putative hydrolase MSMEG_3995/MSMEI_3903;
DE            EC=3.5.-.-;
GN   OrderedLocusNames=MSMEG_3995, MSMEI_3903;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-217, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK75477.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP40361.1; -; Genomic_DNA.
DR   RefSeq; WP_011729456.1; NZ_SIJM01000044.1.
DR   RefSeq; YP_888281.1; NC_008596.1.
DR   AlphaFoldDB; A0QZE3; -.
DR   SMR; A0QZE3; -.
DR   STRING; 246196.MSMEI_3903; -.
DR   EnsemblBacteria; ABK75477; ABK75477; MSMEG_3995.
DR   EnsemblBacteria; AFP40361; AFP40361; MSMEI_3903.
DR   GeneID; 66735355; -.
DR   KEGG; msg:MSMEI_3903; -.
DR   KEGG; msm:MSMEG_3995; -.
DR   PATRIC; fig|246196.19.peg.3934; -.
DR   eggNOG; COG0624; Bacteria.
DR   OMA; YWGSGNM; -.
DR   OrthoDB; 829830at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   PANTHER; PTHR32494; PTHR32494; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01879; hydantase; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Isopeptide bond; Metal-binding; Reference proteome;
KW   Ubl conjugation; Zinc.
FT   CHAIN           1..438
FT                   /note="Putative hydrolase MSMEG_3995/MSMEI_3903"
FT                   /id="PRO_0000396813"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        217
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   438 AA;  47337 MW;  A17D465377113314 CRC64;
     MTVPVNATNL RIPLDTGRDR EFLDSWAELE AIGATPAGGV ERQAGTAEDG QMRDWLSRWL
     RTRGFSVEVD PIGNLFGLLE FNPGAPYVLV GSHLDSQPRG GRFDGAYGVL AGAVAADRTR
     RYVTRSGFTP RYNVAVVDWF NEEGSRFKPS MMGSAVFTGT LDLEEALNTT DDDGVSVRDA
     LAAINGIGDR EVFSSTGPRQ LAAYAEIHIE QGRELEKNNV TIGLVDRTWA ANKYELNVVG
     IQGHTGATAI EDRQDALLGA ALIVVALRDI ADEFGEELHT SCGQLTVLPN SPVVVPREVH
     MHLDLRSDND ELLAAADAAL RRRIAEAEIR AGVKVEHRKA HVWPGHHYQP QGVELARDAA
     NDLGISSMLV QTRAGHDSTN MKEIVPSVML FVPSVEGISH AEAEYTSDED LCSGVDLLTE
     VVARMLDGSL DAAGAGHP