SECBL_MYCTU
ID SECBL_MYCTU Reviewed; 181 AA.
AC P95257; L0TAX4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=SecB-like chaperone Rv1957;
GN Name=secBL; OrderedLocusNames=Rv1957;
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 INDUCTION, DISRUPTION PHENOTYPE, AND OPERON STRUCTURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19118359; DOI=10.1099/mic.0.022889-0;
RA Smollett K.L., Fivian-Hughes A.S., Smith J.E., Chang A., Rao T.,
RA Davis E.O.;
RT "Experimental determination of translational start sites resolves
RT uncertainties in genomic open reading frame predictions - application to
RT Mycobacterium tuberculosis.";
RL Microbiology 155:186-197(2009).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12657046; DOI=10.1046/j.1365-2958.2003.03425.x;
RA Sassetti C.M., Boyd D.H., Rubin E.J.;
RT "Genes required for mycobacterial growth defined by high density
RT mutagenesis.";
RL Mol. Microbiol. 48:77-84(2003).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20585061; DOI=10.1128/jb.00454-10;
RA Fivian-Hughes A.S., Davis E.O.;
RT "Analyzing the regulatory role of the HigA antitoxin within Mycobacterium
RT tuberculosis.";
RL J. Bacteriol. 192:4348-4356(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
RP FUNCTION AS A CHAPERONE, SUBUNIT, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21536872; DOI=10.1073/pnas.1101189108;
RA Bordes P., Cirinesi A.M., Ummels R., Sala A., Sakr S., Bitter W.,
RA Genevaux P.;
RT "SecB-like chaperone controls a toxin-antitoxin stress-responsive system in
RT Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8438-8443(2011).
CC -!- FUNCTION: Chaperone component of an atypical, type II toxin-antitoxin
CC chaperone (TAC) system. Prevents antitoxin HigA1 aggregation in vitro
CC at a 1:3 chaperone:antitoxin ratio, probably also protects antitoxin
CC HigA1 from protease. Required for neutralization of toxin HigB1 upon
CC ectopic expression in Mycobacterium marinum or E.coli. When expressed
CC in E.coli complements a secB deletion, restores export of OmpA and MBP
CC and inhibits aggregation of proOmpC although it is less efficient than
CC endogenous SecB. Complements the general chaperone function of E.coli
CC SecB less well. {ECO:0000269|PubMed:21536872}.
CC -!- SUBUNIT: Homotetramer, interacts with antitoxin HigA1.
CC {ECO:0000269|PubMed:21536872}.
CC -!- INDUCTION: Probably induced by the DNA damaging agent mitomycin C. Part
CC of the Rv1954A-higB1-higA1-Rv1957 operon, as well as the higB1-higA1-
CC Rv1957 operon, which is probably the mitomycin-induced operon; the
CC former but not latter operon is autorepressed by HigA1
CC (PubMed:20585061). {ECO:0000269|PubMed:19118359,
CC ECO:0000269|PubMed:20585061}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in slow growth. A triple
CC higB1-higA1-Rv1957 disruption mutant has no visible phenotype.
CC {ECO:0000269|PubMed:12657046, ECO:0000269|PubMed:19118359}.
CC -!- SIMILARITY: Belongs to the SecB-like family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44725.1; -; Genomic_DNA.
DR PIR; A70639; A70639.
DR RefSeq; NP_216473.1; NC_000962.3.
DR RefSeq; WP_003409891.1; NZ_NVQJ01000048.1.
DR PDB; 5MTW; X-ray; 1.84 A; A/B/C/D=1-181.
DR PDBsum; 5MTW; -.
DR AlphaFoldDB; P95257; -.
DR SMR; P95257; -.
DR STRING; 83332.Rv1957; -.
DR iPTMnet; P95257; -.
DR PaxDb; P95257; -.
DR DNASU; 885961; -.
DR GeneID; 45425927; -.
DR GeneID; 885961; -.
DR KEGG; mtu:Rv1957; -.
DR TubercuList; Rv1957; -.
DR eggNOG; ENOG50339MZ; Bacteria.
DR OMA; DSNFEFA; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR Gene3D; 3.10.420.10; -; 1.
DR InterPro; IPR035958; SecB-like_sf.
DR SUPFAM; SSF54611; SSF54611; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..181
FT /note="SecB-like chaperone Rv1957"
FT /id="PRO_0000407372"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:5MTW"
FT STRAND 23..37
FT /evidence="ECO:0007829|PDB:5MTW"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5MTW"
FT STRAND 47..59
FT /evidence="ECO:0007829|PDB:5MTW"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5MTW"
FT STRAND 65..79
FT /evidence="ECO:0007829|PDB:5MTW"
FT STRAND 96..111
FT /evidence="ECO:0007829|PDB:5MTW"
FT HELIX 122..151
FT /evidence="ECO:0007829|PDB:5MTW"
SQ SEQUENCE 181 AA; 20106 MW; 416F3E9426A48440 CRC64;
MTDRTDADDL DLQRVGARLA ARAQIRDIRL LRTQAAVHRA PKPAQGLTYD LEFEPAVDAD
PATISAFVVR ISCHLRIQNQ AADDDVKEGD TKDETQDVAT ADFEFAALFD YHLQEGEDDP
TEEELTAYAA TTGRFALYPY IREYVYDLTG RLALPPLTLE ILSRPMPVSP GAQWPATRGT
P
