RPFB_MYCTO
ID RPFB_MYCTO Reviewed; 362 AA.
AC P9WG28; F2GHD1; L0T719; O05594; Q7D900;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Resuscitation-promoting factor RpfB;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=rpfB; OrderedLocusNames=MT1038;
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 -!- FUNCTION: Factor that stimulates resuscitation of dormant cells. Has
CC peptidoglycan (PG) hydrolytic activity. PG fragments could either
CC directly activate the resuscitation pathway of dormant bacteria or
CC serve as a substrate for endogenous Rpf, resulting in low molecular
CC weight products with resuscitation activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45288.1; -; Genomic_DNA.
DR PIR; D70603; D70603.
DR RefSeq; WP_003405187.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WG28; -.
DR SMR; P9WG28; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; AAK45288; AAK45288; MT1038.
DR KEGG; mtc:MT1038; -.
DR PATRIC; fig|83331.31.peg.1113; -.
DR HOGENOM; CLU_036884_1_0_11; -.
DR Proteomes; UP000001020; 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 3: Inferred from homology;
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_0000428434"
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