ECCD5_MYCTU
ID ECCD5_MYCTU Reviewed; 503 AA.
AC P9WNP9; L0T9A2; O53944; Q7D7Y4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=ESX-5 secretion system protein EccD5 {ECO:0000305};
DE AltName: Full=ESX conserved component D5 {ECO:0000303|PubMed:19876390};
DE AltName: Full=Type VII secretion system protein EccD5 {ECO:0000305};
DE Short=T7SS protein EccD5 {ECO:0000305};
GN Name=eccD5 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv1795;
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 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 [3]
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=22340629; DOI=10.1111/j.1365-2958.2012.08001.x;
RA Bottai D., Di Luca M., Majlessi L., Frigui W., Simeone R., Sayes F.,
RA Bitter W., Brennan M.J., Leclerc C., Batoni G., Campa M., Brosch R.,
RA Esin S.;
RT "Disruption of the ESX-5 system of Mycobacterium tuberculosis causes loss
RT of PPE protein secretion, reduction of cell wall integrity and strong
RT attenuation.";
RL Mol. Microbiol. 83:1195-1209(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22925462; DOI=10.1111/j.1365-2958.2012.08206.x;
RA Houben E.N., Bestebroer J., Ummels R., Wilson L., Piersma S.R.,
RA Jimenez C.R., Ottenhoff T.H., Luirink J., Bitter W.;
RT "Composition of the type VII secretion system membrane complex.";
RL Mol. Microbiol. 86:472-484(2012).
CC -!- FUNCTION: Part of the ESX-5 specialized secretion system, which is
CC responsible for the secretion of EsxN and a number of PE_PGRS and PPE
CC proteins, including PPE41. {ECO:0000269|PubMed:22340629,
CC ECO:0000269|PubMed:22925462}.
CC -!- SUBUNIT: Part of the ESX-5 / type VII secretion system (T7SS), which is
CC composed of cytosolic and membrane components. The ESX-5 membrane
CC complex is composed of EccB5, EccC5, EccD5 and EccE5.
CC {ECO:0000250|UniProtKB:B2HSU6}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HSU6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutants are defective in the secretion of EsxN,
CC PPE41 and PE_PGRS proteins (PubMed:22340629, PubMed:22925462). Mutant
CC is highly sensitive to detergents and hydrophilic antibiotics such as
CC ampicillin, vancomycin and bacitracin (PubMed:22340629). Virulence is
CC attenuated both in macrophages and in the severe combined immune-
CC deficient mouse infection model (PubMed:22340629).
CC {ECO:0000269|PubMed:22340629, ECO:0000269|PubMed:22925462}.
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; CCP44561.1; -; Genomic_DNA.
DR PIR; D70930; D70930.
DR RefSeq; NP_216311.1; NC_000962.3.
DR RefSeq; WP_003900411.1; NZ_NVQJ01000037.1.
DR PDB; 7NP7; EM; 4.03 A; D1/D2/D3/D4/D5/D6/D7/D8/D9/DA/DB/DC=1-503.
DR PDB; 7NPR; EM; 3.82 A; D1/D2/D3/D4/D5/D6/D7/D8/D9/DA/DB/DC=1-503.
DR PDB; 7NPT; EM; 3.27 A; D7/D8=1-503.
DR PDB; 7NPU; EM; 4.48 A; D1/D2/D3/D4/D5/D6/D7/D8/D9/DA/DB/DC=1-503.
DR PDB; 7NPV; EM; 6.66 A; D1/D2/D3/D4/D5/D6/D7/D8/D9/DA/DB/DC=1-503.
DR PDBsum; 7NP7; -.
DR PDBsum; 7NPR; -.
DR PDBsum; 7NPT; -.
DR PDBsum; 7NPU; -.
DR PDBsum; 7NPV; -.
DR AlphaFoldDB; P9WNP9; -.
DR SMR; P9WNP9; -.
DR STRING; 83332.Rv1795; -.
DR PaxDb; P9WNP9; -.
DR DNASU; 885628; -.
DR GeneID; 45425772; -.
DR GeneID; 885628; -.
DR KEGG; mtu:Rv1795; -.
DR TubercuList; Rv1795; -.
DR eggNOG; ENOG502ZAY5; Bacteria.
DR OMA; WIRFIPD; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR InterPro; IPR044049; EccD_transm.
DR InterPro; IPR006707; T7SS_EccD.
DR InterPro; IPR024962; YukD-like.
DR Pfam; PF19053; EccD; 1.
DR Pfam; PF08817; YukD; 1.
DR PIRSF; PIRSF017804; Secretion_EccD1; 1.
DR TIGRFAMs; TIGR03920; T7SS_EccD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..503
FT /note="ESX-5 secretion system protein EccD5"
FT /id="PRO_0000393237"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 503 AA; 53435 MW; 80C27906BA60DEF3 CRC64;
MTAVADAPQA DIEGVASPQA VVVGVMAGEG VQIGVLLDAN APVSVMTDPL LKVVNSRLRE
LGEAPLEATG RGRWALCLVD GAPLRATQSL TEQDVYDGDR LWIRFIADTE RRSQVIEHIS
TAVASDLSKR FARIDPIVAV QVGASMVATG VVLATGVLGW WRWHHNTWLT TIYTAVIGVL
VLAVAMLLLM RAKTDADRRV ADIMLMSAIM PVTVAAAAAP PGPVGSPQAV LGFGVLTVAA
ALALRFTGRR LGIYTTIVII GALTMLAALA RMVAATSAVT LLSSLLLICV VAYHAAPALS
RRLAGIRLPV FPSATSRWVF EARPDLPTTV VVSGGSAPVL EGPSSVRDVL LQAERARSFL
SGLLTGLGVM VVVCMTSLCD PHTGQRWLPL ILAGFTSGFL LLRGRSYVDR WQSITLAGTA
VIIAAAVCVR YALELSSPLA VSIVAAILVL LPAAGMAAAA HVPHTIYSPL FRKFVEWIEY
LCLMPIFPLA LWLMNVYAAI RYR
