RIPA_MYCS2
ID RIPA_MYCS2 Reviewed; 497 AA.
AC A0QX22;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Peptidoglycan endopeptidase RipA;
DE EC=3.4.-.-;
DE AltName: Full=Resuscitation-promoting factor interaction partner A;
DE Short=Rpf-interacting protein A;
DE Flags: Precursor;
GN Name=ripA; OrderedLocusNames=MSMEG_3145, MSMEI_3064;
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 FUNCTION IN CELL DIVISION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18463693; DOI=10.1371/journal.ppat.1000001;
RA Hett E.C., Chao M.C., Deng L.L., Rubin E.J.;
RT "A mycobacterial enzyme essential for cell division synergizes with
RT resuscitation-promoting factor.";
RL PLoS Pathog. 4:E1000001-E1000001(2008).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=22610443; DOI=10.1074/jbc.m112.346544;
RA Plocinska R., Purushotham G., Sarva K., Vadrevu I.S., Pandeeti E.V.,
RA Arora N., Plocinski P., Madiraju M.V., Rajagopalan M.;
RT "Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase
RT promotes MtrA regulon expression.";
RL J. Biol. Chem. 287:23887-23899(2012).
CC -!- FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-
CC glutamate and meso-diaminopimelate. Binds and degrades high-molecular
CC weight peptidoglycan. Required for normal separation of daughter cells
CC after cell division and for cell wall integrity (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:18463693}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Localizes to the septa.
CC {ECO:0000250}.
CC -!- INDUCTION: Expression depends on the two-component regulatory system
CC MtrA/MtrB. {ECO:0000269|PubMed:22610443}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted. Depletion
CC experiments show cells grow as long, branched chains that form clumps.
CC Periodic septa and DNA segregation appear to occur normally along the
CC filaments. Has increased susceptibility to carbenicillin, a cell wall-
CC targeted antibiotic. Depletion effects are reversible.
CC {ECO:0000269|PubMed:18463693}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; CP000480; ABK70310.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39528.1; -; Genomic_DNA.
DR RefSeq; WP_011728845.1; NZ_SIJM01000002.1.
DR RefSeq; YP_887460.1; NC_008596.1.
DR AlphaFoldDB; A0QX22; -.
DR SMR; A0QX22; -.
DR STRING; 246196.MSMEI_3064; -.
DR EnsemblBacteria; ABK70310; ABK70310; MSMEG_3145.
DR EnsemblBacteria; AFP39528; AFP39528; MSMEI_3064.
DR GeneID; 66734546; -.
DR KEGG; msg:MSMEI_3064; -.
DR KEGG; msm:MSMEG_3145; -.
DR PATRIC; fig|246196.19.peg.3106; -.
DR eggNOG; COG0791; Bacteria.
DR eggNOG; COG3883; Bacteria.
DR OMA; RTSRDQY; -.
DR OrthoDB; 682655at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IMP:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071554; P:cell wall organization or biogenesis; IGI:UniProtKB.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Thiol protease.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..497
FT /note="Peptidoglycan endopeptidase RipA"
FT /id="PRO_0000421120"
FT DOMAIN 365..497
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 177..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 457
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ SEQUENCE 497 AA; 51317 MW; 2556CF24316C2381 CRC64;
MRRTVRALAT RVHGRVCAVP LVVGMLLATA LYGGGPAAAD PAAPDNLATL VAKVASADQK
LQELGAAIQT QQETVNKAIV DVQAARDAAA AAQRELEAGQ RGVADANAAI EAAQKRFDSF
AAATYMNGPS RSYLTATDPA DIVNTTATGQ ALIASSQQVM AKLQRARTEQ VNRESAARLA
KEKADQAARD AESSQDNAVA ALKQAQQTFN AQQGELERLA AERAAAQAEL DSVRKVSATG
NAAPAAAPAA APAPAAAPAP VPNSAPAPVP GAQPNPQAAA GNWDRAPSGP ASSGQNWAVW
DPTLPAIPSA FVSGDPIAII NAVLGIASTS AQVTADMGRS FLQKLGILPT PTGFTNGAIP
RVYGREAVEY VIRRGMSQIG VPYSWGGGNA AGPSRGIDSG AGTVGFDCSG LMLYMFAGVG
IKLDHYSGSQ YNAGRKIPSS QMRRGDMIFY GPNASQHVAM YLGNGQMLEA PYTGSHVKVS
PVRTSGMTPY VTRLIEY
