ID   RPFB_MYCTE              Reviewed;         362 AA.
AC   H8EZH5;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Resuscitation-promoting factor RpfB;
DE            EC=3.-.-.-;
DE   Flags: Precursor;
GN   Name=rpfB; OrderedLocusNames=ERDMAN_1122;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=16622237; DOI=10.1128/iai.74.5.2985-2995.2006;
RA   Tufariello J.M., Mi K., Xu J., Manabe Y.C., Kesavan A.K., Drumm J.,
RA   Tanaka K., Jacobs W.R. Jr., Chan J.;
RT   "Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor
RT   Rv1009 gene results in delayed reactivation from chronic tuberculosis.";
RL   Infect. Immun. 74:2985-2995(2006).
CC   -!- FUNCTION: Factor that stimulates resuscitation of dormant cells. Has
CC       peptidoglycan (PG) hydrolytic activity. Active in the pM concentration
CC       range. Has little to no effect on actively-growing cells. PG fragments
CC       could either directly activate the resuscitation pathway of dormant
CC       bacteria or serve as a substrate for endogenous Rpf, resulting in low
CC       molecular weight products with resuscitation activity (By similarity).
CC       Plays a role in reactivating bacteria from chronic tuberculosis (TB) in
CC       mice. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: In infected C57BL/6 mice levels remains constant following
CC       reactivation of TB (induced by the nitric oxide synthase inhibitor
CC       aminoguanidine) for 4 weeks then decreases over 10-fold until at least
CC       11 weeks. {ECO:0000269|PubMed:16622237}.
CC   -!- DISRUPTION PHENOTYPE: No difference in chronic C57BL/6 mouse infection,
CC       but infected mice show delayed reactivation of TB (induced by
CC       aminoguanidine, a nitric oxide synthase inhibitor) compared to mice
CC       infected with wild-type bacteria. Bacterial loads in lung, liver, and
CC       spleen are similar during chronic infection, but increase more slowly
CC       in the disrupted mutant after reactivation. Pulmonary B-cell responses
CC       are reduced in mice infected with the disrupted strain at advanced
CC       stages of TB reactivation. While disease is delayed, it does eventually
CC       occur, suggesting other the Rpfs compensate.
CC       {ECO:0000269|PubMed:16622237}.
CC   -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP012340; BAL64927.1; -; Genomic_DNA.
DR   RefSeq; WP_003405187.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8EZH5; -.
DR   SMR; H8EZH5; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; BAL64927; BAL64927; ERDMAN_1122.
DR   KEGG; mtn:ERDMAN_1122; -.
DR   PATRIC; fig|652616.3.peg.1135; -.
DR   HOGENOM; CLU_036884_1_0_11; -.
DR   Proteomes; UP000007568; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:UniProt.
DR   GO; GO:0040010; P:positive regulation of growth rate; IEA:UniProt.
DR   CDD; cd13925; RPF; 1.
DR   InterPro; IPR007137; DUF348.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR010618; RPF.
DR   Pfam; PF03990; DUF348; 3.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF06737; Transglycosylas; 1.
DR   SMART; SM01208; G5; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51109; G5; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Signal; Virulence.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           24..362
FT                   /note="Resuscitation-promoting factor RpfB"
FT                   /id="PRO_0000421027"
FT   DOMAIN          192..272
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   DISULFID        291..355
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  38078 MW;  02B55D8C70373D10 CRC64;
     MLRLVVGALL LVLAFAGGYA VAACKTVTLT VDGTAMRVTT MKSRVIDIVE ENGFSVDDRD
     DLYPAAGVQV HDADTIVLRR SRPLQISLDG HDAKQVWTTA STVDEALAQL AMTDTAPAAA
     SRASRVPLSG MALPVVSAKT VQLNDGGLVR TVHLPAPNVA GLLSAAGVPL LQSDHVVPAA
     TAPIVEGMQI QVTRNRIKKV TERLPLPPNA RRVEDPEMNM SREVVEDPGV PGTQDVTFAV
     AEVNGVETGR LPVANVVVTP AHEAVVRVGT KPGTEVPPVI DGSIWDAIAG CEAGGNWAIN
     TGNGYYGGVQ FDQGTWEANG GLRYAPRADL ATREEQIAVA EVTRLRQGWG AWPVCAARAG
     AR