ID   Y2915_MYCTO             Reviewed;         370 AA.
AC   P9WL22; L0TDX9; P68917; Q10965;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Uncharacterized protein MT2982.1;
GN   OrderedLocusNames=MT2982.1;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE000516; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C70747; C70747.
DR   RefSeq; WP_003899537.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WL22; -.
DR   SMR; P9WL22; -.
DR   GeneID; 45426902; -.
DR   PATRIC; fig|83331.31.peg.3223; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..370
FT                   /note="Uncharacterized protein MT2982.1"
FT                   /id="PRO_0000427554"
SQ   SEQUENCE   370 AA;  39770 MW;  8F9887DE1C3D64B9 CRC64;
     MKRVDTIRPR SRAVRLHVRG LGLPDETAIQ LWIVDGRIST EPVAGADTVF DGGWILPGLV
     DAHCHVGLGK HGNVELDEAI AQAETERDVG ALLLRDCGSP TDTRGLDDHE DLPRIIRAGR
     HLARPKRYIA GFAVELEDES QLPAAVAEQA RRGDGWVKLV GDWIDRQIGD LAPLWSDDVL
     KAAIDTAHAQ GARVTAHVFS EDALPGLINA GIDCIEHGTG LTDDTIALML EHGTALVPTL
     INLENFPGIA DAAGRYPTYA AHMRDLYARG YGRVAAAREA GVPVYAGTDA GSTIEHGRIA
     DEVAALQRIG MTAHEALGAA CWDARRWLGR PGLDDRASAD LLCYAQDPRQ GPGVLQHPDL
     VILRGRTFGP