ECCD3_MYCTU
ID ECCD3_MYCTU Reviewed; 472 AA.
AC P9WNQ3; L0T326; O86362; Q7DA32;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=ESX-3 secretion system protein EccD3 {ECO:0000305};
DE AltName: Full=ESX conserved component D3 {ECO:0000305};
DE AltName: Full=Type VII secretion system protein EccD3 {ECO:0000305};
DE Short=T7SS protein EccD3 {ECO:0000305};
GN Name=eccD3 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv0290;
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.
RX PubMed=12065475; DOI=10.1128/iai.70.7.3371-3381.2002;
RA Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.;
RT "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in
RT iron-dependent gene expression, iron metabolism, and oxidative stress
RT response.";
RL Infect. Immun. 70:3371-3381(2002).
RN [3]
RP INDUCTION.
RX PubMed=17098899; DOI=10.1128/jb.01190-06;
RA Maciag A., Dainese E., Rodriguez G.M., Milano A., Provvedi R., Pasca M.R.,
RA Smith I., Palu G., Riccardi G., Manganelli R.;
RT "Global analysis of the Mycobacterium tuberculosis Zur (FurB) regulon.";
RL J. Bacteriol. 189:730-740(2007).
RN [4]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [5]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=19684129; DOI=10.1128/jb.00756-09;
RA Serafini A., Boldrin F., Palu G., Manganelli R.;
RT "Characterization of a Mycobacterium tuberculosis ESX-3 conditional mutant:
RT essentiality and rescue by iron and zinc.";
RL J. Bacteriol. 191:6340-6344(2009).
RN [6]
RP NOMENCLATURE.
RX PubMed=19876390; DOI=10.1371/journal.ppat.1000507;
RA Bitter W., Houben E.N., Bottai D., Brodin P., Brown E.J., Cox J.S.,
RA Derbyshire K., Fortune S.M., Gao L.Y., Liu J., Gey van Pittius N.C.,
RA Pym A.S., Rubin E.J., Sherman D.R., Cole S.T., Brosch R.;
RT "Systematic genetic nomenclature for type VII secretion systems.";
RL PLoS Pathog. 5:E1000507-E1000507(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [8]
RP FUNCTION.
RX PubMed=24155985; DOI=10.1371/journal.pone.0078351;
RA Serafini A., Pisu D., Palu G., Rodriguez G.M., Manganelli R.;
RT "The ESX-3 secretion system is necessary for iron and zinc homeostasis in
RT Mycobacterium tuberculosis.";
RL PLoS ONE 8:E78351-E78351(2013).
CC -!- FUNCTION: Part of the ESX-3 specialized secretion system, which is
CC important for iron and zinc uptake or homeostasis.
CC {ECO:0000269|PubMed:19684129, ECO:0000269|PubMed:24155985}.
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:B2HSU6}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HSU6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Repressed by IdeR in the presence of iron and by Zur in the
CC presence of zinc. {ECO:0000269|PubMed:12065475,
CC ECO:0000269|PubMed:17098899}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the EccD/Snm4 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43020.1; -; Genomic_DNA.
DR PIR; H70836; H70836.
DR RefSeq; NP_214804.1; NC_000962.3.
DR RefSeq; WP_003401524.1; NZ_NVQJ01000026.1.
DR AlphaFoldDB; P9WNQ3; -.
DR SMR; P9WNQ3; -.
DR STRING; 83332.Rv0290; -.
DR PaxDb; P9WNQ3; -.
DR DNASU; 886599; -.
DR GeneID; 886599; -.
DR KEGG; mtu:Rv0290; -.
DR PATRIC; fig|83332.111.peg.326; -.
DR TubercuList; Rv0290; -.
DR eggNOG; ENOG5031ZT8; Bacteria.
DR OMA; WDSAPCK; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR InterPro; IPR006707; T7SS_EccD.
DR InterPro; IPR024962; YukD-like.
DR Pfam; PF08817; YukD; 1.
DR PIRSF; PIRSF017804; Secretion_EccD1; 1.
DR TIGRFAMs; TIGR03920; T7SS_EccD; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..472
FT /note="ESX-3 secretion system protein EccD3"
FT /id="PRO_0000393235"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 47944 MW; 2A132D3AB0A7F3D1 CRC64;
MSGTVMQIVR VAILADSRLT EMALPAELPL REILPAVQRL VVPSAQNGDG GQADSGAAVQ
LSLAPVGGQP FSLDASLDTV GVVDGDLLVL QPVPAGPAAP GIVEDIADAA MIFSTSRLKP
WGIAHIQRGA LAAVIAVALL ATGLTVTYRV ATGVLAGLLA VAGIAVASAL AGLLITIRSP
RSGIALSIAA LVPIGAALAL AVPGKFGPAQ VLLGAAGVAA WSLIALMIPS AERERVVAFF
TAAAVVGASV ALAAGAQLLW QLPLLSIGCG LIVAALLVTI QAAQLSALWA RFPLPVIPAP
GDPTPSAPPL RLLEDLPRRV RVSDAHQSGF IAAAVLLSVL GSVAIAVRPE ALSVVGWYLV
AATAAAATLR ARVWDSAACK AWLLAQPYLV AGVLLVFYTA TGRYVAAFGA VLVLAVLMLA
WVVVALNPGI ASPESYSLPL RRLLGLVAAG LDVSLIPVMA YLVGLFAWVL NR
