ID   Y3950_MYCS2             Reviewed;         294 AA.
AC   A0QZA1; I7G3Z8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Universal stress protein MSMEG_3950/MSMEI_3859;
DE            Short=USP MSMEG_3950;
GN   OrderedLocusNames=MSMEG_3950, MSMEI_3859;
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-109, 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   -!- SIMILARITY: Belongs to the universal stress protein A family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK73928.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP40317.1; -; Genomic_DNA.
DR   RefSeq; WP_003895405.1; NZ_SIJM01000005.1.
DR   RefSeq; YP_888239.1; NC_008596.1.
DR   AlphaFoldDB; A0QZA1; -.
DR   SMR; A0QZA1; -.
DR   STRING; 246196.MSMEI_3859; -.
DR   PRIDE; A0QZA1; -.
DR   EnsemblBacteria; ABK73928; ABK73928; MSMEG_3950.
DR   EnsemblBacteria; AFP40317; AFP40317; MSMEI_3859.
DR   GeneID; 66735315; -.
DR   KEGG; msg:MSMEI_3859; -.
DR   KEGG; msm:MSMEG_3950; -.
DR   PATRIC; fig|246196.19.peg.3890; -.
DR   eggNOG; COG0589; Bacteria.
DR   OMA; VATHASC; -.
DR   OrthoDB; 2040681at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR006015; Universal_stress_UspA.
DR   InterPro; IPR006016; UspA.
DR   Pfam; PF00582; Usp; 2.
DR   PRINTS; PR01438; UNVRSLSTRESS.
PE   1: Evidence at protein level;
KW   ATP-binding; Isopeptide bond; Nucleotide-binding; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..294
FT                   /note="Universal stress protein MSMEG_3950/MSMEI_3859"
FT                   /id="PRO_0000396945"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         117..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         131..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         261..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         275..277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   CROSSLNK        109
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   294 AA;  31452 MW;  3CC1A9C3C8BA2790 CRC64;
     MVQSATEYGI LVGVDSSAES DAAVRWAARE ASLHDAPITL MHVIAPVVVS WPAGPYMATV
     LECQEENARH AIEQAQKVVA DCLGETHGLT VQTEIRKESV ARTLIDASKS AQMVVVGNRG
     MGALGRVLLG STSTSLLHYA SGPVVVVHGD DQAAHDSRLP VLLGIDGSPA SEVATSHAFD
     EASRRGVDLV ALHVWIDVGD IPPIGPTWEE QEETGRALLA ERLAGWQERY PDVKVHRRVE
     RAQPAYWLLE EAKQAQLVVV GSHGRGGFTG MLLGSVSSRV AQSATTPVMV VRPR