ECCB3_MYCS2
ID ECCB3_MYCS2 Reviewed; 518 AA.
AC A0QQ39;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=ESX-3 secretion system ATPase EccB3 {ECO:0000250|UniProtKB:P9WNR3};
DE EC=3.6.-.- {ECO:0000305};
DE AltName: Full=ESX conserved component B3 {ECO:0000250|UniProtKB:P9WNR3};
DE AltName: Full=Type VII secretion system protein EccB3 {ECO:0000250|UniProtKB:P9WNR3};
DE Short=T7SS protein EccB3 {ECO:0000250|UniProtKB:P9WNR3};
GN Name=eccB3 {ECO:0000303|PubMed:24803520};
GN OrderedLocusNames=MSMEG_0616 {ECO:0000312|EMBL:ABK75660.1},
GN MSMEI_0600 {ECO:0000312|EMBL:AFP37081.1};
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 FUNCTION.
RX PubMed=19846780; DOI=10.1073/pnas.0900589106;
RA Siegrist M.S., Unnikrishnan M., McConnell M.J., Borowsky M., Cheng T.Y.,
RA Siddiqi N., Fortune S.M., Moody D.B., Rubin E.J.;
RT "Mycobacterial Esx-3 is required for mycobactin-mediated iron
RT acquisition.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18792-18797(2009).
RN [5]
RP FUNCTION.
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).
CC -!- FUNCTION: An ATPase (By similarity). Part of the ESX-3 specialized
CC secretion system, which is required for siderophore-mediated iron
CC acquisition and for the secretion of EsxH and EsxG.
CC {ECO:0000250|UniProtKB:P9WNR7, ECO:0000269|PubMed:19846780,
CC ECO:0000269|PubMed:24803520}.
CC -!- SUBUNIT: Part of the ESX-3 / type VII secretion system (T7SS), which is
CC composed of cytosolic and membrane components. The ESX-3 membrane
CC complex is composed of EccB3, EccC3, EccD3 and EccE3.
CC {ECO:0000250|UniProtKB:B2HST3}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HST3}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR EMBL; CP000480; ABK75660.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37081.1; -; Genomic_DNA.
DR RefSeq; WP_003892036.1; NZ_SIJM01000009.1.
DR RefSeq; YP_885027.1; NC_008596.1.
DR PDB; 6LAR; EM; 3.70 A; A/I=1-518.
DR PDB; 6SGW; EM; 3.80 A; A/I=9-91.
DR PDB; 6SGX; EM; 3.70 A; A=11-89.
DR PDB; 6SGY; EM; 4.60 A; A/B=100-518.
DR PDB; 6SGZ; EM; 3.90 A; I=33-91.
DR PDB; 6UMM; EM; 3.70 A; D/I=13-93.
DR PDBsum; 6LAR; -.
DR PDBsum; 6SGW; -.
DR PDBsum; 6SGX; -.
DR PDBsum; 6SGY; -.
DR PDBsum; 6SGZ; -.
DR PDBsum; 6UMM; -.
DR AlphaFoldDB; A0QQ39; -.
DR SMR; A0QQ39; -.
DR STRING; 246196.MSMEI_0600; -.
DR PRIDE; A0QQ39; -.
DR EnsemblBacteria; ABK75660; ABK75660; MSMEG_0616.
DR EnsemblBacteria; AFP37081; AFP37081; MSMEI_0600.
DR GeneID; 66738794; -.
DR KEGG; msg:MSMEI_0600; -.
DR KEGG; msm:MSMEG_0616; -.
DR PATRIC; fig|246196.19.peg.612; -.
DR eggNOG; COG3266; Bacteria.
DR OMA; WTVCDAV; -.
DR OrthoDB; 311112at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.910; -; 1.
DR Gene3D; 3.30.2390.20; -; 1.
DR InterPro; IPR007795; T7SS_EccB.
DR InterPro; IPR044857; T7SS_EccB_R1.
DR InterPro; IPR042485; T7SS_EccB_R3.
DR PANTHER; PTHR40765; PTHR40765; 1.
DR Pfam; PF05108; T7SS_ESX1_EccB; 1.
DR TIGRFAMs; TIGR03919; T7SS_EccB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Hydrolase;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="ESX-3 secretion system ATPase EccB3"
FT /id="PRO_0000434990"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 53638 MW; 9C241B9952C8C50A CRC64;
MTGPVNPDDR RSFSSRTPVN ENPDGVQYRR GFVTRHQVSG WRFVMRRIAS GVALHDTRML
VDPLRTQSRA VLTGALILVT GLVGCFIFSL FRPGGVPGNN AILADRSTSA LYVRVGEQLH
PVLNLTSARL ISGSPDNPTM VKTSEIDKFP RGNLLGIPGA PERMVQNAAT DAEWTVCDAV
GGANPGVTVI AGPLGADGER AAPLPPDHAV LVHSDAEPNP GDWLLWDGKR SPIDLADRAV
TDALGLGGQA LAPRPIAAGL FNAVPAAPAL TAPVIPDAGA APQFELSLPV PVGAVVVAYD
ADNTARYYAV LSDGLQPISP VLAAILRNTD SHGFAQPPRL GPDEVARTPM SRGLDTSAYP
DNPVTLVEAS AHPVTCAHWT KPSDAAESSL SVLSGAVLPL AEGLHTVDLV GAGAGGAANR
VALTPGTGYF VQTVGAEPGS PTAGSMFWVS DTGVRYGIDT AEDDKVVAAL GLSTSPLPVP
WSVLSQFAAG PALSRGDALV AHDAVSTNPN SARMEASR
