ECCC3_MYCTU
ID ECCC3_MYCTU Reviewed; 1330 AA.
AC P9WNA9; L0T4X3; O53689; Q7DA37;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=ESX-3 secretion system protein EccC3 {ECO:0000305};
DE AltName: Full=ESX conserved component C3 {ECO:0000305};
DE AltName: Full=Type VII secretion system protein EccC3 {ECO:0000305};
DE Short=T7SS protein EccC3 {ECO:0000305};
GN Name=eccC3 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv0284;
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:B2HST4}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HST4}; 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 ---------------------------------------------------------------------------
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; AL123456; CCP43014.1; -; Genomic_DNA.
DR PIR; B70836; B70836.
DR RefSeq; NP_214798.1; NC_000962.3.
DR RefSeq; WP_003916637.1; NZ_NVQJ01000026.1.
DR PDB; 6J17; X-ray; 1.98 A; A=1052-1330.
DR PDBsum; 6J17; -.
DR AlphaFoldDB; P9WNA9; -.
DR SMR; P9WNA9; -.
DR STRING; 83332.Rv0284; -.
DR PaxDb; P9WNA9; -.
DR PRIDE; P9WNA9; -.
DR DNASU; 886611; -.
DR GeneID; 886611; -.
DR KEGG; mtu:Rv0284; -.
DR TubercuList; Rv0284; -.
DR eggNOG; COG1672; Bacteria.
DR eggNOG; COG1674; Bacteria.
DR OMA; DGIYDPP; -.
DR PhylomeDB; P9WNA9; -.
DR PHI-base; PHI:5577; -.
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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR023836; EccCa-like_Actinobacteria.
DR InterPro; IPR023837; EccCb-like_Actinobacteria.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 3.
DR TIGRFAMs; TIGR03924; T7SS_EccC_a; 1.
DR TIGRFAMs; TIGR03925; T7SS_EccC_b; 1.
DR PROSITE; PS50901; FTSK; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1330
FT /note="ESX-3 secretion system protein EccC3"
FT /id="PRO_0000393430"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 456..662
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 811..1000
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 1090..1280
FT /note="FtsK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 479..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 829..836
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 1107..1114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT STRAND 1064..1066
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1068..1071
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1080..1086
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1087..1089
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1092..1096
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1097..1099
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1102..1106
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1113..1126
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1130..1132
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1133..1138
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1143..1146
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1154..1156
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1159..1161
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1162..1174
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1183..1186
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1187..1189
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1196..1201
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1224..1227
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1228..1235
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1238..1244
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1249..1255
FT /evidence="ECO:0007829|PDB:6J17"
FT HELIX 1257..1264
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1268..1271
FT /evidence="ECO:0007829|PDB:6J17"
FT TURN 1276..1279
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1294..1298
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1300..1302
FT /evidence="ECO:0007829|PDB:6J17"
FT STRAND 1305..1310
FT /evidence="ECO:0007829|PDB:6J17"
SQ SEQUENCE 1330 AA; 145170 MW; C7D09C3067EE751B CRC64;
MSRLIFEARR RLAPPSSHQG TIIIEAPPEL PRVIPPSLLR RALPYLIGIL IVGMIVALVA
TGMRVISPQT LFFPFVLLLA ATALYRGNDK KMRTEEVDAE RADYLRYLSV VRDNIRAQAA
EQRASALWSH PDPTALASVP GSRRQWERDP HDPDFLVLRA GRHTVPLATT LRVNDTADEI
DLEPVSHSAL RSLLDTQRSI GDVPTGIDLT KVSPITVLGE RAQVRAVLRA WIAQAVTWHD
PTVLGVALAA RDLEGRDWNW LKWLPHVDIP GRLDALGPAR NLSTDPDELI ALLGPVLADR
PAFTGQPTDA LRHLLIVVDD PDYDLGASPL AVGRAGVTVV HCSASAPHRE QYSDPEKPIL
RVAHGAIERW QTGGWQPYID AADQFSADEA AHLARRLSRW DSNPTHAGLR SAATRGASFT
TLLGIEDASR LDVPALWAPR RRDEELRVPI GVTGTGEPLM FDLKDEAEGG MGPHGLMIGM
TGSGKSQTLM SILLSLLTTH SAERLIVIYA DFKGEAGADS FRDFPQVVAV ISNMAEKKSL
ADRFADTLRG EVARREMLLR EAGRKVQGSA FNSVLEYENA IAAGHSLPPI PTLFVVADEF
TLMLADHPEY AELFDYVARK GRSFRIHILF ASQTLDVGKI KDIDKNTAYR IGLKVASPSV
SRQIIGVEDA YHIESGKEHK GVGFLVPAPG ATPIRFRSTY VDGIYEPPQT AKAVVVQSVP
EPKLFTAAAV EPDPGTVIAD TDEQEPADPP RKLIATIGEQ LARYGPRAPQ LWLPPLDETI
PLSAALARAG VGPRQWRWPL GEIDRPFEMR RDPLVFDARS SAGNMVIHGG PKSGKSTALQ
TFILSAASLH SPHEVSFYCL DYGGGQLRAL QDLAHVGSVA SALEPERIRR TFGELEQLLL
SRQQREVFRD RGANGSTPDD GFGEVFLVID NLYGFGRDNT DQFNTRNPLL ARVTELVNVG
LAYGIHVIIT TPSWLEVPLA MRDGLGLRLE LRLHDARDSN VRVVGALRRP ADAVPHDQPG
RGLTMAAEHF LFAAPELDAQ TNPVAAINAR YPGMAAPPVR LLPTNLAPHA VGELYRGPDQ
LVIGQREEDL APVILDLAAN PLLMVFGDAR SGKTTLLRHI IRTVREHSTA DRVAFTVLDR
RLHLVDEPLF PDNEYTANID RIIPAMLGLA NLIEARRPPA GMSAAELSRW TFAGHTHYLI
IDDVDQVPDS PAMTGPYIGQ RPWTPLIGLL AQAGDLGLRV IVTGRATGSA HLLMTSPLLR
RFNDLQATTL MLAGNPADSG KIRGERFARL PAGRAILLTD SDSPTYVQLI NPLVDAAAVS
GETQQKGSQS
