ECCA3_MYCS2
ID ECCA3_MYCS2 Reviewed; 608 AA.
AC A0QQ38; I7F659;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ESX-3 secretion system protein EccA3 {ECO:0000250|UniProtKB:P9WPI3};
DE AltName: Full=ESX conserved component A3 {ECO:0000250|UniProtKB:P9WPI3};
DE AltName: Full=Type VII secretion system protein EccA3 {ECO:0000250|UniProtKB:P9WPI3};
DE Short=T7SS protein EccA3 {ECO:0000250|UniProtKB:P9WPI3};
GN Name=eccA3 {ECO:0000303|PubMed:24803520};
GN OrderedLocusNames=MSMEG_0615 {ECO:0000312|EMBL:ABK69981.1},
GN MSMEI_0599 {ECO:0000312|EMBL:AFP37080.1};
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: Part of the ESX-3 specialized secretion system, which is
CC required for siderophore-mediated iron acquisition and for the
CC secretion of EsxH and EsxG (PubMed:19846780, PubMed:24803520). EccA3
CC exhibits ATPase activity and may provide energy for the export of ESX-3
CC substrates (By similarity). {ECO:0000250|UniProtKB:P9WPH9,
CC ECO:0000269|PubMed:19846780, 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.
CC {ECO:0000250|UniProtKB:P9WPH9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU9}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK69981.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK69981.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP37080.1; -; Genomic_DNA.
DR RefSeq; YP_885026.1; NC_008596.1.
DR PDB; 7NAZ; X-ray; 1.60 A; A=21-300.
DR PDBsum; 7NAZ; -.
DR AlphaFoldDB; A0QQ38; -.
DR SMR; A0QQ38; -.
DR STRING; 246196.MSMEI_0599; -.
DR EnsemblBacteria; ABK69981; ABK69981; MSMEG_0615.
DR EnsemblBacteria; AFP37080; AFP37080; MSMEI_0599.
DR KEGG; msg:MSMEI_0599; -.
DR KEGG; msm:MSMEG_0615; -.
DR PATRIC; fig|246196.19.peg.611; -.
DR eggNOG; COG0464; Bacteria.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041627; AAA_lid_6.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023835; T7SS_EccA.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17866; AAA_lid_6; 1.
DR PRINTS; PR00819; CBXCFQXSUPER.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03922; T7SS_EccA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..608
FT /note="ESX-3 secretion system protein EccA3"
FT /id="PRO_0000434989"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 608 AA; 66283 MW; 568BAE5FDA2DD329 CRC64;
MGSDTLAAPP HGAPRVDRDV VSRFATCCRA LGLTVNDRQR PADLTAARAG FAGLTHLAHD
QCDAWIGLAA AGEVTPAVVD AVWRTVASAG VLQREIGLAA GELGFTYDTG WYLQFRATEP
DDFQLAYAAR LYEAGEFGEA DGLVGEILAR RPGWFDARWL QVAINHRAQR WSDVVRLLTP
VVTLPSLDDV TSHAVRTALG ISLARLGMFA PAMSYLEDPA GPIEVAAVDG ALAKALTLRA
QGEDDEATEV LQDLFATHPE NTQVEQALLD TSFGLVTTTS ARIEARSDPW DPETEPSEAE
FVDPGAKDRK AHLLLEAEAE LAEFIGLEEV KFQVARLKSS VAMAIRRQER GLAVAQRTNH
LVFAGPPGTG KTTIARVVAK IYCGLGLLKK ETVREVHRAD LIGQHIGETE AKTNAIIDSA
LDGVLFLDEA YALVSTGAKN DFGLVAIDTL LARMENDRDR LVVIVAGYRK DLDAFLDTNE
GLRSRFTRSI DFPSYTAPEL VEIAVRMAEK RDSVFEKAAH DDMERLFTHL AQATTPDANG
VERRSLDIAG NARFVRNLVE RSEEEREYRL DHSDQEDFTD EEMMTITAGD VQRSAAPLLR
GLGLSVPA
