RIPB_MYCTU
ID RIPB_MYCTU Reviewed; 241 AA.
AC P9WHU5; L0T9R3; O53169; Q7D8D5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Peptidoglycan endopeptidase RipB;
DE EC=3.4.-.-;
DE AltName: Full=Macrophage invasion and intracellular persistence protein B;
DE AltName: Full=Resuscitation-promoting factor interaction partner B;
DE Short=Rpf-interacting protein B;
DE Flags: Precursor;
GN Name=ripB; OrderedLocusNames=Rv1478;
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 FUNCTION IN HOST CELL INVASION, AND MUTAGENESIS OF 188-ARG--ASP-200.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16495549; DOI=10.1128/iai.74.3.1757-1767.2006;
RA Gao L.Y., Pak M., Kish R., Kajihara K., Brown E.J.;
RT "A mycobacterial operon essential for virulence in vivo and invasion and
RT intracellular persistence in macrophages.";
RL Infect. Immun. 74:1757-1767(2006).
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 X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 30-241, CATALYTIC ACTIVITY,
RP PEPTIDOGLYCAN BINDING, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE
RP SITE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21864539; DOI=10.1016/j.jmb.2011.08.014;
RA Both D., Schneider G., Schnell R.;
RT "Peptidoglycan remodeling in Mycobacterium tuberculosis: comparison of
RT structures and catalytic activities of RipA and RipB.";
RL J. Mol. Biol. 413:247-260(2011).
CC -!- FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-
CC glutamate and meso-diaminopimelate. Binds high-molecular weight
CC peptidoglycan, but does not degrade it. Required for normal separation
CC of daughter cells after cell division and cell wall integrity. Required
CC for host cell invasion. {ECO:0000269|PubMed:16495549}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:21864539};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21864539}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; AL123456; CCP44238.1; -; Genomic_DNA.
DR PIR; A70874; A70874.
DR RefSeq; NP_215994.1; NC_000962.3.
DR RefSeq; WP_003407525.1; NZ_NVQJ01000004.1.
DR PDB; 3PBI; X-ray; 1.60 A; A=30-241.
DR PDBsum; 3PBI; -.
DR AlphaFoldDB; P9WHU5; -.
DR SMR; P9WHU5; -.
DR STRING; 83332.Rv1478; -.
DR PaxDb; P9WHU5; -.
DR DNASU; 886535; -.
DR GeneID; 45425457; -.
DR GeneID; 886535; -.
DR KEGG; mtu:Rv1478; -.
DR TubercuList; Rv1478; -.
DR eggNOG; COG0791; Bacteria.
DR OMA; GANRIPR; -.
DR PhylomeDB; P9WHU5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3D-structure; Cell wall biogenesis/degradation; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..241
FT /note="Peptidoglycan endopeptidase RipB"
FT /id="PRO_0000413763"
FT DOMAIN 109..241
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284,
FT ECO:0000269|PubMed:21864539"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284,
FT ECO:0000269|PubMed:21864539"
FT ACT_SITE 213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284,
FT ECO:0000305|PubMed:21864539"
FT MUTAGEN 188..190
FT /note="RGD->AGA: Abolishes host cell invasion."
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 60..80
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:3PBI"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:3PBI"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3PBI"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3PBI"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3PBI"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3PBI"
SQ SEQUENCE 241 AA; 24624 MW; C4DFAA6A4863BA7A CRC64;
MRHTRFHPIK LAWITAVVAG LMVGVATPAD AEPGQWDPTL PALVSAGAPG DPLAVANASL
QATAQATQTT LDLGRQFLGG LGINLGGPAA SAPSAATTGA SRIPRANARQ AVEYVIRRAG
SQMGVPYSWG GGSLQGPSKG VDSGANTVGF DCSGLVRYAF AGVGVLIPRF SGDQYNAGRH
VPPAEAKRGD LIFYGPGGGQ HVTLYLGNGQ MLEASGSAGK VTVSPVRKAG MTPFVTRIIE
Y
