ECCB5_MYCTU
ID ECCB5_MYCTU Reviewed; 506 AA.
AC P9WNQ9; L0TAD6; O53933; Q7D7Z1;
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-5 secretion system ATPase EccB5 {ECO:0000305};
DE EC=3.6.-.- {ECO:0000305};
DE AltName: Full=ESX conserved component B5 {ECO:0000303|PubMed:19876390};
DE AltName: Full=Type VII secretion system protein EccB5 {ECO:0000305};
DE Short=T7SS protein EccB5 {ECO:0000305};
GN Name=eccB5 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv1782;
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 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 [3]
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 [4]
RP FUNCTION.
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 [5]
RP FUNCTION.
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).
RN [6]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=23284869; DOI=10.1371/journal.pone.0052059;
RA Di Luca M., Bottai D., Batoni G., Orgeur M., Aulicino A., Counoupas C.,
RA Campa M., Brosch R., Esin S.;
RT "The ESX-5 associated eccB-EccC locus is essential for Mycobacterium
RT tuberculosis viability.";
RL PLoS ONE 7:E52059-E52059(2012).
RN [7]
RP FUNCTION AS AN ATPASE.
RC STRAIN=H37Rv;
RX PubMed=26396239; DOI=10.1096/fj.15-270843;
RA Zhang X.L., Li D.F., Fleming J., Wang L.W., Zhou Y., Wang D.C., Zhang X.E.,
RA Bi L.J.;
RT "Core component EccB1 of the Mycobacterium tuberculosis type VII secretion
RT system is a periplasmic ATPase.";
RL FASEB J. 29:4804-4814(2015).
CC -!- FUNCTION: An ATPase (shown for residues 80-506) (PubMed:26396239). Part
CC of the ESX-5 specialized secretion system, which is responsible for the
CC secretion of EsxN and a number of PE_PGRS and PPE proteins, including
CC PPE41. {ECO:0000269|PubMed:22340629, ECO:0000269|PubMed:22925462,
CC ECO:0000269|PubMed:23284869}.
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:B2HST3}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HST3}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: Part of the eccB5-eccC5 operon, which is essential for
CC in vitro growth. {ECO:0000269|PubMed:23284869}.
CC -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44549.1; -; Genomic_DNA.
DR PIR; H70928; H70928.
DR RefSeq; NP_216298.1; NC_000962.3.
DR RefSeq; WP_003899021.1; NZ_NVQJ01000037.1.
DR PDB; 7NP7; EM; 4.03 A; B1/B2/B3/B4/B5/B6=1-506.
DR PDB; 7NPR; EM; 3.82 A; B1/B2/B3/B4/B5/B6=1-506.
DR PDB; 7NPS; EM; 3.81 A; B1/B2/B3/B4/B5/B6=1-506.
DR PDB; 7NPU; EM; 4.48 A; B1/B2/B3/B4/B5/B6=1-506.
DR PDB; 7NPV; EM; 6.66 A; B1/B2/B3/B4/B5/B6=1-506.
DR PDBsum; 7NP7; -.
DR PDBsum; 7NPR; -.
DR PDBsum; 7NPS; -.
DR PDBsum; 7NPU; -.
DR PDBsum; 7NPV; -.
DR AlphaFoldDB; P9WNQ9; -.
DR SMR; P9WNQ9; -.
DR STRING; 83332.Rv1782; -.
DR PaxDb; P9WNQ9; -.
DR DNASU; 885347; -.
DR GeneID; 885347; -.
DR KEGG; mtu:Rv1782; -.
DR TubercuList; Rv1782; -.
DR eggNOG; COG3266; Bacteria.
DR OMA; TESLWWL; -.
DR PhylomeDB; P9WNQ9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Disulfide bond; Hydrolase; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..506
FT /note="ESX-5 secretion system ATPase EccB5"
FT /id="PRO_0000393232"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..506
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT DISULFID 162..363
FT /evidence="ECO:0000250|UniProtKB:P9WNR7"
SQ SEQUENCE 506 AA; 53721 MW; 07116CB384B2814D CRC64;
MAEESRGQRG SGYGLGLSTR TQVTGYQFLA RRTAMALTRW RVRMEIEPGR RQTLAVVASV
SAALVICLGA LLWSFISPSG QLNESPIIAD RDSGALYVRV GDRLYPALNL ASARLITGRP
DNPHLVRSSQ IATMPRGPLV GIPGAPSSFS PKSPPASSWL VCDTVATSSS IGSLQGVTVT
VIDGTPDLTG HRQILSGSDA VVLRYGGDAW VIREGRRSRI EPTNRAVLLP LGLTPEQVSQ
ARPMSRALFD ALPVGPELLV PEVPNAGGPA TFPGAPGPIG TVIVTPQISG PQQYSLVLGD
GVQTLPPLVA QILQNAGSAG NTKPLTVEPS TLAKMPVVNR LDLSAYPDNP LEVVDIREHP
STCWWWERTA GENRARVRVV SGPTIPVAAT EMNKVVSLVK ADTSGRQADQ VYFGPDHANF
VAVTGNNPGA QTSESLWWVT DAGARFGVED SKEARDALGL TLTPSLAPWV ALRLLPQGPT
LSRADALVEH DTLPMDMTPA ELVVPK
