RPF2_CORGL
ID RPF2_CORGL Reviewed; 374 AA.
AC Q6M6N7; Q8NRY2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Resuscitation-promoting factor Rpf2;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=rpf2; OrderedLocusNames=Cgl0909, cg1037;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP POSSIBLE CLEAVAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15480574; DOI=10.1007/s00203-004-0713-1;
RA Hartmann M., Barsch A., Niehaus K., Puhler A., Tauch A., Kalinowski J.;
RT "The glycosylated cell surface protein Rpf2, containing a resuscitation-
RT promoting factor motif, is involved in intercellular communication of
RT Corynebacterium glutamicum.";
RL Arch. Microbiol. 182:299-312(2004).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15090522; DOI=10.1128/jb.186.9.2798-2809.2004;
RA Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.;
RT "RamB, a novel transcriptional regulator of genes involved in acetate
RT metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 186:2798-2809(2004).
RN [5]
RP ISOFORMS, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16734784; DOI=10.1111/j.1574-6968.2006.00269.x;
RA Mahne M., Tauch A., Puhler A., Kalinowski J.;
RT "The Corynebacterium glutamicum gene pmt encoding a glycosyltransferase
RT related to eukaryotic protein-O-mannosyltransferases is essential for
RT glycosylation of the resuscitation promoting factor (Rpf2) and other
RT secreted proteins.";
RL FEMS Microbiol. Lett. 259:226-233(2006).
RN [6]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18355281; DOI=10.1111/j.1574-6968.2008.01098.x;
RA Jungwirth B., Emer D., Brune I., Hansmeier N., Puehler A., Eikmanns B.J.,
RA Tauch A.;
RT "Triple transcriptional control of the resuscitation promoting factor 2
RT (rpf2) gene of Corynebacterium glutamicum by the regulators of acetate
RT metabolism RamA and RamB and the cAMP-dependent regulator GlxR.";
RL FEMS Microbiol. Lett. 281:190-197(2008).
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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cell surface {ECO:0000305}.
CC -!- INDUCTION: Activated by RamA and repressed by RamB.
CC {ECO:0000269|PubMed:15090522, ECO:0000269|PubMed:18355281}.
CC -!- PTM: Glycosylated; by Pmt, by at least mannose and galactose. Other
CC unidentified sugars may also be present. {ECO:0000269|PubMed:15480574,
CC ECO:0000269|PubMed:16734784}.
CC -!- PTM: May be subject to proteolytic cleavage as multiple shorter forms
CC are detected in gels.
CC -!- PTM: At least 3 non-glycosylated protein isoforms of 35, 40 and 42 kDa
CC are seen in gels. {ECO:0000269|PubMed:16734784}.
CC -!- DISRUPTION PHENOTYPE: Not essential; a double rpf1-rpf2 disruption
CC mutant is also viable. The double mutant displays a prolonged lag phase
CC and slower growth after transfer of long-stored cells into fresh
CC medium. {ECO:0000269|PubMed:15480574}.
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98302.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000036; BAB98302.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927150; CAF19615.1; -; Genomic_DNA.
DR RefSeq; NP_600137.1; NC_003450.3.
DR RefSeq; WP_003858490.1; NC_006958.1.
DR AlphaFoldDB; Q6M6N7; -.
DR SMR; Q6M6N7; -.
DR STRING; 196627.cg1037; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR DNASU; 3342641; -.
DR GeneID; 58311215; -.
DR KEGG; cgb:cg1037; -.
DR KEGG; cgl:Cgl0909; -.
DR PATRIC; fig|196627.13.peg.894; -.
DR eggNOG; COG3583; Bacteria.
DR HOGENOM; CLU_036884_1_0_11; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..374
FT /note="Resuscitation-promoting factor Rpf2"
FT /id="PRO_0000421070"
FT DOMAIN 210..290
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT REGION 228..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 38966 MW; 01973001F08B8A7B CRC64;
MAPHQKSRIN RINSTRSVPL RLATGGVLAT LLIGGVTAAA TKKDIIVDVN GEQMSLVTMS
GTVEGVLAQA GVELGDQDIV SPSLDSSISD EDTVTVRTAK QVALVVEGQI QNVTTTAVSV
EDLLQEVGGI TGADAVDADL SETIPESGLK VSVTKPKIIS INDGGKVTYV SLAAQNVQEA
LELRDIELGA QDRINVPLDQ QLKNNAAIQI DRVDNTEITE TVSFDAEPTY VDDPEAPAGD
ETVVEEGAPG TKEVTRTVTT VNGQEESSTV INEVEITAAK PATISRGTKT VAANSVWDQL
AQCESGGNWA INTGNGFSGG LQFHPQTWLA YGGGAFSGDA SGASREQQIS IAEKVQAAQG
WGAWPACTAS LGIR
