ID   Y3034_MYCTU             Reviewed;         300 AA.
AC   O53281; L0TEA3;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable acetyltransferase Rv3034c {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000305};
DE   AltName: Full=Peroxisome homeostasis protein Rv3034c {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rv3034c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
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.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., 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]
RP   PUTATIVE FUNCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17640872; DOI=10.1074/jbc.m702676200;
RA   Stadthagen G., Sambou T., Guerin M., Barilone N., Boudou F.,
RA   Kordulakova J., Charles P., Alzari P.M., Lemassu A., Daffe M., Puzo G.,
RA   Gicquel B., Riviere M., Jackson M.;
RT   "Genetic basis for the biosynthesis of methylglucose lipopolysaccharides in
RT   Mycobacterium tuberculosis.";
RL   J. Biol. Chem. 282:27270-27276(2007).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
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).
RN   [4]
RP   FUNCTION IN VIRULENCE.
RC   STRAIN=H37Rv;
RX   PubMed=32388919; DOI=10.1111/cmi.13214;
RA   Ganguli G., Pattanaik K.P., Jagadeb M., Sonawane A.;
RT   "Mycobacterium tuberculosis Rv3034c regulates mTORC1 and PPAR-gamma
RT   dependant pexophagy mechanism to control redox levels in macrophages.";
RL   Cell. Microbiol. 22:e13214-e13214(2020).
CC   -!- FUNCTION: May be involved in the biosynthesis of 6-O-methylglucosyl-
CC       containing lipopolysaccharides (MGLP). {ECO:0000305|PubMed:17640872}.
CC   -!- FUNCTION: Regulates host peroxisome homeostasis in response to
CC       intracellular redox levels to favor mycobacterial infection in
CC       macrophage (PubMed:32388919). Induces the expression of host peroxisome
CC       biogenesis and proliferation factors as well as peroxisome associated
CC       enzymes. Inhibits the induction of host pexophagy mechanism by down-
CC       regulating the expression of pexophagy associated proteins and adapter
CC       molecules in infected macrophages. However, during increased oxidative
CC       stress conditions, it induces degradation of dysfunctional and damaged
CC       peroxisomes. Regulation of peroxisome biogenesis and degradation is
CC       dependent upon host p-mTORC1 mediated signaling pathway
CC       (PubMed:32388919). {ECO:0000269|PubMed:32388919}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45843.1; -; Genomic_DNA.
DR   PIR; E70859; E70859.
DR   RefSeq; NP_217550.1; NC_000962.3.
DR   RefSeq; WP_003902399.1; NC_000962.3.
DR   AlphaFoldDB; O53281; -.
DR   SMR; O53281; -.
DR   STRING; 83332.Rv3034c; -.
DR   PaxDb; O53281; -.
DR   DNASU; 887470; -.
DR   GeneID; 887470; -.
DR   KEGG; mtu:Rv3034c; -.
DR   PATRIC; fig|83332.111.peg.3381; -.
DR   TubercuList; Rv3034c; -.
DR   eggNOG; COG0110; Bacteria.
DR   InParanoid; O53281; -.
DR   OMA; MEIGRWV; -.
DR   PhylomeDB; O53281; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Repeat; Signal; Transferase;
KW   Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..300
FT                   /note="Probable acetyltransferase Rv3034c"
FT                   /id="PRO_0000413012"
SQ   SEQUENCE   300 AA;  33064 MW;  9C7A5C12673D0C8D CRC64;
     MNVLSLGSSS GVVWGRVPIT APAGAATGVT SRADAHSQMR RYAQTGPTAK LSSAPMTTMW
     GAPLHRRWRG SRLRDPRQAK FLTLASLKWV LANRAYTPWY LVRYWRLLRF KLANPHIITR
     GMVFLGKGVE IHATPELAQL EIGRWVHIGD KNTIRAHEGS LRFGDKVVLG RDNVINTYLD
     IEIGDSVLMA DWCYICDFDH RMDDITLPIK DQGIIKSPVR IGPDTWIGVK VSVLRGTTIG
     RGCVLGSHAV VRGAIPDYSI AVGAPAKVVK NRQLSWEASA AQRAELAAAL ADIERKKAAR