ESXB_THECD
ID ESXB_THECD Reviewed; 104 AA.
AC D1A4H0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=ESAT-6-like protein {ECO:0000255|RuleBase:RU362001};
GN Name=esxB {ECO:0000303|PubMed:25865481}; OrderedLocusNames=Tcur_0610;
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC Thermomonospora.
OX NCBI_TaxID=471852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goeker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
RN [2] {ECO:0007744|PDB:4LWS, ECO:0007744|PDB:4N1A}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-104 IN COMPLEX WITH ESXA, X-RAY
RP CRYSTALLOGRAPHY (3.24 ANGSTROMS) OF 82-104 IN COMPLEX WITH ECCC C-TERMINUS,
RP FUNCTION, INTERACTION WITH ECCC AND ESXA, SUBUNIT, AND MUTAGENESIS OF
RP TYR-84; GLU-88; 98-VAL--GLY-104; VAL-98 AND LEU-102.
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=25865481; DOI=10.1016/j.cell.2015.03.040;
RA Rosenberg O.S., Dovala D., Li X., Connolly L., Bendebury A.,
RA Finer-Moore J., Holton J., Cheng Y., Stroud R.M., Cox J.S.;
RT "Substrates control multimerization and activation of the multi-domain
RT ATPase motor of type VII secretion.";
RL Cell 161:501-512(2015).
CC -!- FUNCTION: May help regulate assembly and function of the type VII
CC secretion system (T7SS). Binds to EccC and induces its multimerization
CC (PubMed:25865481). May serve as a chaperone for EsxA (By similarity).
CC {ECO:0000250|UniProtKB:P9WNK5, ECO:0000269|PubMed:25865481}.
CC -!- SUBUNIT: In isolation forms a homodimer (PubMed:25865481). Forms a
CC tight 1:1 complex with EsxA (PubMed:25865481). Forms a complex with
CC EsxA and EccC, probably wholly mediated by EsxB; binds in a pocket in
CC the third FtsK (ATPase) domain of EccC (residues 1163-1208)
CC (PubMed:25865481). {ECO:0000269|PubMed:25865481}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WNK5}.
CC Note=Probably secreted via the ESX / type VII secretion system (T7SS).
CC {ECO:0000305|PubMed:25865481}.
CC -!- SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP001738; ACY96205.1; -; Genomic_DNA.
DR PDB; 4LWS; X-ray; 2.00 A; A=2-104.
DR PDB; 4N1A; X-ray; 3.24 A; G/H/J/K=82-104.
DR PDBsum; 4LWS; -.
DR PDBsum; 4N1A; -.
DR AlphaFoldDB; D1A4H0; -.
DR SMR; D1A4H0; -.
DR STRING; 471852.Tcur_0610; -.
DR EnsemblBacteria; ACY96205; ACY96205; Tcur_0610.
DR KEGG; tcu:Tcur_0610; -.
DR eggNOG; COG4842; Bacteria.
DR HOGENOM; CLU_151185_2_0_11; -.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR036689; ESAT-6-like_sf.
DR InterPro; IPR010310; T7SS_ESAT-6-like.
DR Pfam; PF06013; WXG100; 1.
DR SUPFAM; SSF140453; SSF140453; 1.
DR TIGRFAMs; TIGR03930; WXG100_ESAT6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Reference proteome; Secreted.
FT CHAIN 1..104
FT /note="ESAT-6-like protein"
FT /id="PRO_0000438303"
FT COILED 12..43
FT /evidence="ECO:0000255"
FT MUTAGEN 84
FT /note="Y->A: Still activates EccC A-543 ATPase activity."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 88
FT /note="E->A: Still activates EccC A-543 ATPase activity."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 98..104
FT /note="VQALLNG->LLSQMGF: Interacts with M.tuberculosis
FT EccCb1 instead of endogenous EccC, still interacts with
FT endogenous EsxA, mutations change binding site to that of
FT M.tuberculosis."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 98
FT /note="V->A: Peptide of residues 95-104 no longer disrupts
FT EsxA-EsxB complex, does not activate ATPase activity of
FT mutant EccC A-543."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 102
FT /note="L->A: Peptide of residues 95-104 no longer disrupts
FT EsxA-EsxB complex."
FT /evidence="ECO:0000269|PubMed:25865481"
FT HELIX 5..42
FT /evidence="ECO:0007829|PDB:4LWS"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:4LWS"
FT HELIX 53..92
FT /evidence="ECO:0007829|PDB:4LWS"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:4LWS"
SQ SEQUENCE 104 AA; 11511 MW; FEE5AB7B6044FA17 CRC64;
MAPQSAVDRA AMAQAAQDIE QSANAIRGMQ NQLASAKDQL RSHWEGDASM AFEAVFNRFN
EDFSRVLKAL DGMHESLVQT RITYEAREEA AQQSVNRVQA LLNG
