ID P72062_MYCTU Unreviewed; 375 AA.
AC P72062; F2GDF5; I6YD19; L0TGS6;
DT 01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 2.
DT 27-MAR-2024, entry version 137.
DE SubName: Full=Conserved protein {ECO:0000313|EMBL:CCP46625.1};
GN Name=atsH {ECO:0000313|EMBL:CCP46625.1};
GN OrderedLocusNames=Rv3796 {ECO:0000313|EMBL:CCP46625.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP46625.1, ECO:0000313|Proteomes:UP000001584};
RN [1] {ECO:0000313|EMBL:CCP46625.1, ECO:0000313|Proteomes:UP000001584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584};
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J.,
RA Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2] {ECO:0007829|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.M111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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DR EMBL; AL123456; CCP46625.1; -; Genomic_DNA.
DR RefSeq; WP_003420646.1; NZ_NVQJ01000009.1.
DR RefSeq; YP_178016.1; NC_000962.3.
DR AlphaFoldDB; P72062; -.
DR SMR; P72062; -.
DR STRING; 83332.Rv3796; -.
DR PaxDb; 83332-Rv3796; -.
DR DNASU; 886128; -.
DR GeneID; 45427798; -.
DR GeneID; 886128; -.
DR KEGG; mtu:Rv3796; -.
DR PATRIC; fig|83332.111.peg.4221; -.
DR eggNOG; COG1234; Bacteria.
DR InParanoid; P72062; -.
DR OrthoDB; 4137979at2; -.
DR PhylomeDB; P72062; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR CDD; cd07719; arylsulfatase_AtsA-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR044094; AtsA-like_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR46018:SF8; RIBONUCLEASE Z; 1.
DR PANTHER; PTHR46018; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 1: Evidence at protein level;
KW Reference proteome {ECO:0000313|Proteomes:UP000001584}.
FT DOMAIN 81..126
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF00753"
FT DOMAIN 231..342
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 375 AA; 39444 MW; 7089700EB8715308 CRC64;
MLLGMHQAGH VGTHERRAAA TRRSALTAAG LAVVGAGVLG ASACSPQKSP QPSSPRLPDN
ALITLGVAAG PPPTPSRVGI SSVLKIGRDL YVIDCGLGSL NAFTNAGLQF DDLKAMFITH
LHTDHIVDYY NFFLSGGFLA PPGRAPVLVY GPGPAGGLPP SEVGNPNPAT VNPANPTPGL
AAATEALHRA FAYTSNIFIR DYGIDNVADL VKVTEIGLPP GSDYRNRAPK MSPFSVASDD
NVSVTATLVS HYDVYPAFGF RFDLKKSGVS VTFSGDTTKS DNLITLAQGT DILVHEAVFS
LDTAYFGNAF PPNYLVNSHT SAEQVGEVAA AAKPKQLILS HYAPDDLPDS QWLDKIKKNY
SGMTTIARDG QVFAL
//
