ECCA3_MYCTU
ID ECCA3_MYCTU Reviewed; 631 AA.
AC P9WPI3; L0T677; O53687;
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 EccA3 {ECO:0000305};
DE AltName: Full=ESX conserved component A3 {ECO:0000305};
DE AltName: Full=Type VII secretion system protein EccA3 {ECO:0000305};
DE Short=T7SS protein EccA3 {ECO:0000305};
GN Name=eccA3 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv0282;
GN ORFNames=MTV035.10;
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 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 [5]
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 [6]
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 [7]
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 (PubMed:19684129,
CC PubMed:24155985). EccA3 exhibits ATPase activity and may provide energy
CC for the export of ESX-3 substrates (By similarity).
CC {ECO:0000250|UniProtKB:P9WPH9, ECO:0000269|PubMed:19684129,
CC 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.
CC {ECO:0000250|UniProtKB:P9WPH9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU9}.
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 -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43012.1; -; Genomic_DNA.
DR PIR; H70835; H70835.
DR RefSeq; NP_214796.1; NC_000962.3.
DR RefSeq; WP_003898392.1; NC_000962.3.
DR AlphaFoldDB; P9WPI3; -.
DR SMR; P9WPI3; -.
DR STRING; 83332.Rv0282; -.
DR PaxDb; P9WPI3; -.
DR DNASU; 886613; -.
DR GeneID; 886613; -.
DR KEGG; mtu:Rv0282; -.
DR PATRIC; fig|83332.111.peg.318; -.
DR TubercuList; Rv0282; -.
DR eggNOG; COG0464; Bacteria.
DR OMA; AHEQCDA; -.
DR PhylomeDB; P9WPI3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; 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:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:MTBBASE.
DR GO; GO:0055072; P:iron ion homeostasis; IDA:MTBBASE.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:MTBBASE.
DR GO; GO:0055069; P:zinc ion homeostasis; IDA:MTBBASE.
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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03922; T7SS_EccA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..631
FT /note="ESX-3 secretion system protein EccA3"
FT /id="PRO_0000063045"
FT BINDING 385..392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 68107 MW; BE4D492E351C6C53 CRC64;
MAGVGEGDSG GVERDDIGMV AASPVASRVN GKVDADVVGR FATCCRALGI AVYQRKRPPD
LAAARSGFAA LTRVAHDQCD AWTGLAAAGD QSIGVLEAAS RTATTAGVLQ RQVELADNAL
GFLYDTGLYL RFRATGPDDF HLAYAAALAS TGGPEEFAKA NHVVSGITER RAGWRAARWL
AVVINYRAER WSDVVKLLTP MVNDPDLDEA FSHAAKITLG TALARLGMFA PALSYLEEPD
GPVAVAAVDG ALAKALVLRA HVDEESASEV LQDLYAAHPE NEQVEQALSD TSFGIVTTTA
GRIEARTDPW DPATEPGAED FVDPAAHERK AALLHEAELQ LAEFIGLDEV KRQVSRLKSS
VAMELVRKQR GLTVAQRTHH LVFAGPPGTG KTTIARVVAK IYCGLGLLKR ENIREVHRAD
LIGQHIGETE AKTNAIIDSA LDGVLFLDEA YALVATGAKN DFGLVAIDTL LARMENDRDR
LVVIIAGYRA DLDKFLDTNE GLRSRFTRNI DFPSYTSHEL VEIAHKMAEQ RDSVFEQSAL
HDLEALFAKL AAESTPDTNG ISRRSLDIAG NGRFVRNIVE RSEEEREFRL DHSEHAGSGE
FSDEELMTIT ADDVGRSVEP LLRGLGLSVR A