ESPG3_MYCS2
ID ESPG3_MYCS2 Reviewed; 293 AA.
AC A0QQ45;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=ESX-3 secretion-associated protein EspG3 {ECO:0000305};
GN Name=espG3 {ECO:0000303|PubMed:24803520};
GN OrderedLocusNames=MSMEG_0622 {ECO:0000312|EMBL:ABK72998.1},
GN MSMEI_0606 {ECO:0000312|EMBL:AFP37087.1};
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 DISRUPTION PHENOTYPE.
RX PubMed=24803520; DOI=10.1128/mbio.01073-14;
RA Siegrist M.S., Steigedal M., Ahmad R., Mehra A., Dragset M.S.,
RA Schuster B.M., Philips J.A., Carr S.A., Rubin E.J.;
RT "Mycobacterial Esx-3 requires multiple components for iron acquisition.";
RL MBio 5:E01073-E01073(2014).
RN [5] {ECO:0007744|PDB:4L4W}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS).
RA Korotkov K.V.;
RT "Structure of the ESX secretion system protein.";
RL Submitted (JUN-2013) to the PDB data bank.
RN [6] {ECO:0007744|PDB:4W4J}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RX PubMed=25275011; DOI=10.1073/pnas.1409345111;
RA Ekiert D.C., Cox J.S.;
RT "Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals
RT molecular specificity of ESX protein secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14758-14763(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU5}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene impairs iron-bound
CC mycobactin utilization and EsxG and EsxH export.
CC {ECO:0000269|PubMed:24803520}.
CC -!- SIMILARITY: Belongs to the EspG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK72998.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37087.1; -; Genomic_DNA.
DR RefSeq; WP_011727072.1; NZ_SIJM01000009.1.
DR RefSeq; YP_885033.1; NC_008596.1.
DR PDB; 4L4W; X-ray; 2.04 A; A/B=1-293.
DR PDB; 4RCL; X-ray; 2.70 A; A/B=1-293.
DR PDB; 4W4J; X-ray; 2.80 A; A/B=1-293.
DR PDB; 5SXL; X-ray; 2.46 A; A=1-293.
DR PDBsum; 4L4W; -.
DR PDBsum; 4RCL; -.
DR PDBsum; 4W4J; -.
DR PDBsum; 5SXL; -.
DR AlphaFoldDB; A0QQ45; -.
DR SASBDB; A0QQ45; -.
DR SMR; A0QQ45; -.
DR STRING; 246196.MSMEI_0606; -.
DR EnsemblBacteria; ABK72998; ABK72998; MSMEG_0622.
DR EnsemblBacteria; AFP37087; AFP37087; MSMEI_0606.
DR KEGG; msg:MSMEI_0606; -.
DR KEGG; msm:MSMEG_0622; -.
DR PATRIC; fig|246196.19.peg.618; -.
DR eggNOG; ENOG5030P1E; Bacteria.
DR OMA; DGPWFPD; -.
DR OrthoDB; 638117at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR025734; EspG.
DR Pfam; PF14011; ESX-1_EspG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..293
FT /note="ESX-3 secretion-associated protein EspG3"
FT /id="PRO_0000435129"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:4L4W"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4W4J"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:4L4W"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4RCL"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4L4W"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:4L4W"
SQ SEQUENCE 293 AA; 31637 MW; E1A086F19C8D306E CRC64;
MGPNAVELTT DQAWCLADVL GAGSYPWVLA ITPPYSDHSQ RSAFLAAQSA ELTRMGVVNS
AGAVDPRVAQ WITTVCRATQ WLDLRFVSGP GDLLRGMVAR RSEETVVALR NAQLVTFTAM
DIGHQHALVP VLTAGLSGRK PARFDDFALP AAAGARADEQ IRNGAPLAEV LEFLGVPPSA
RPLVESVFDG RRTYVEIVAG EHRDGHRVTT EVGVSIIDTP HGRILVHPTK AFDGEWISTF
TPGSADAIAM AVERLTASLP SGSWFPDQPL TRDFDEDAAT HREPVLQRRT QKA
