ECCB3_MYCTU
ID ECCB3_MYCTU Reviewed; 538 AA.
AC P9WNR3; L0T5Z9; O53688; Q7DA38;
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 ATPase EccB3 {ECO:0000305};
DE EC=3.6.-.- {ECO:0000305};
DE AltName: Full=ESX conserved component B3 {ECO:0000305};
DE AltName: Full=Type VII secretion system protein EccB3 {ECO:0000305};
DE Short=T7SS protein EccB3 {ECO:0000305};
GN Name=eccB3 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv0283;
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: An ATPase (By similarity). Part of the ESX-3 specialized
CC secretion system, which is important for iron and zinc uptake or
CC homeostasis. {ECO:0000250|UniProtKB:P9WNR7,
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:B2HST3}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HST3}; Single-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 -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43013.1; -; Genomic_DNA.
DR PIR; A70836; A70836.
DR RefSeq; NP_214797.1; NC_000962.3.
DR RefSeq; WP_003401472.1; NZ_NVQJ01000026.1.
DR AlphaFoldDB; P9WNR3; -.
DR SMR; P9WNR3; -.
DR STRING; 83332.Rv0283; -.
DR PaxDb; P9WNR3; -.
DR DNASU; 886645; -.
DR GeneID; 886645; -.
DR KEGG; mtu:Rv0283; -.
DR TubercuList; Rv0283; -.
DR eggNOG; COG3266; Bacteria.
DR OMA; WTVCDAV; -.
DR PhylomeDB; P9WNR3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.910; -; 1.
DR Gene3D; 3.30.2390.20; -; 1.
DR InterPro; IPR007795; T7SS_EccB.
DR InterPro; IPR044857; T7SS_EccB_R1.
DR InterPro; IPR042485; T7SS_EccB_R3.
DR PANTHER; PTHR40765; PTHR40765; 1.
DR Pfam; PF05108; T7SS_ESX1_EccB; 1.
DR TIGRFAMs; TIGR03919; T7SS_EccB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..538
FT /note="ESX-3 secretion system ATPase EccB3"
FT /id="PRO_0000393230"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 55943 MW; DDE9A080B8E67D03 CRC64;
MTNQQHDHDF DHDRRSFASR TPVNNNPDKV VYRRGFVTRH QVTGWRFVMR RIAAGIALHD
TRMLVDPLRT QSRAVLMGVL IVITGLIGSF VFSLIRPNGQ AGSNAVLADR STAALYVRVG
EQLHPVLNLT SARLIVGRPV SPTTVKSTEL DQFPRGNLIG IPGAPERMVQ NTSTDANWTV
CDGLNAPSRG GADGVGVTVI AGPLEDTGAR AAALGPGQAV LVDSGAGTWL LWDGKRSPID
LADHAVTSGL GLGADVPAPR IIASGLFNAI PEAPPLTAPI IPDAGNPASF GVPAPIGAVV
SSYALKDSGK TISDTVQYYA VLPDGLQQIS PVLAAILRNN NSYGLQQPPR LGADEVAKLP
VSRVLDTRRY PSEPVSLVDV TRDPVTCAYW SKPVGAATSS LTLLAGSALP VPDAVHTVEL
VGAGNGGVAT RVALAAGTGY FTQTVGGGPD APGAGSLFWV SDTGVRYGID NEPQGVAGGG
KAVEALGLNP PPVPIPWSVL SLFVPGPTLS RADALLAHDT LVPDSRPARP VSAEGGYR