ECCB1_MYCS2
ID ECCB1_MYCS2 Reviewed; 479 AA.
AC A0QNJ0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=ESX-1 secretion system ATPase EccB1;
GN Name=eccB1 {ECO:0000303|PubMed:19876390};
GN Synonyms=Ms3869 {ECO:0000303|PubMed:15314236},
GN Sm3869 {ECO:0000303|PubMed:15687187}, snm6 {ECO:0000303|PubMed:15687187};
GN OrderedLocusNames=MSMEG_0060, MSMEI_0061;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=15314236; DOI=10.1073/pnas.0404892101;
RA Flint J.L., Kowalski J.C., Karnati P.K., Derbyshire K.M.;
RT "The RD1 virulence locus of Mycobacterium tuberculosis regulates DNA
RT transfer in Mycobacterium smegmatis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12598-12603(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=15687187; DOI=10.1128/jb.187.4.1238-1245.2005;
RA Converse S.E., Cox J.S.;
RT "A protein secretion pathway critical for Mycobacterium tuberculosis
RT virulence is conserved and functional in Mycobacterium smegmatis.";
RL J. Bacteriol. 187:1238-1245(2005).
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 FUNCTION AS AN ATPASE.
RC STRAIN=ATCC 700084 / mc(2)155;
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).
RN [8] {ECO:0007744|PDB:5CYU}
RP X-RAY CRYSTALLOGRAPHY (3.07 ANGSTROMS) OF 73-479, DOMAIN, TOPOLOGY, AND
RP DISULFIDE BOND.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26922638; DOI=10.1186/s12900-016-0056-6;
RA Wagner J.M., Chan S., Evans T.J., Kahng S., Kim J., Arbing M.A.,
RA Eisenberg D., Korotkov K.V.;
RT "Structures of EccB1 and EccD1 from the core complex of the mycobacterial
RT ESX-1 type VII secretion system.";
RL BMC Struct. Biol. 16:5-5(2016).
CC -!- FUNCTION: An ATPase (shown for residues 72-479) (PubMed:26396239). Part
CC of the ESX-1 / type VII specialized secretion system (T7SS), which
CC exports several proteins including EsxA and EsxB (PubMed:15687187).
CC Plays a role in DNA conjugation, in both donor and recipient strains
CC (PubMed:15314236). {ECO:0000269|PubMed:15314236,
CC ECO:0000269|PubMed:15687187, ECO:0000269|PubMed:26396239}.
CC -!- SUBUNIT: Part of the ESX-1 / type VII secretion system (T7SS), which is
CC composed of cytosolic and membrane components. The ESX-1 membrane
CC complex is composed of EccB1, EccCa1, EccCb1, EccD1 and EccE1 (By
CC similarity). {ECO:0000250|UniProtKB:P9WNR7,
CC ECO:0000305|PubMed:19876390}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: Has a discontinuous central core of beta sheets stabilized by a
CC disulfide bond that is flanked by 2 structural domain repeats on each
CC side; the protein forms an elongated 'S'-shaped structure
CC (PubMed:26922638). {ECO:0000269|PubMed:26922638}.
CC -!- DISRUPTION PHENOTYPE: Increases efficiency of DNA conjugation when
CC disrupted in donor strain (PubMed:15314236). Loss of secretion of EsxA
CC and EsxB, but not their expression (PubMed:15687187).
CC {ECO:0000269|PubMed:15314236, ECO:0000269|PubMed:15687187}.
CC -!- MISCELLANEOUS: DNA conjugation in M.smegmatis is unidirectional with
CC distinct donor and recipient strains; mc(2)155 is a donor strain while
CC MKD8 is a recipient strain. Mutations in a donor strain that alter DNA
CC transfer do not always alter DNA transfer in a recipient strain.
CC {ECO:0000305|PubMed:15314236}.
CC -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR EMBL; CP000480; ABK72695.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36543.1; -; Genomic_DNA.
DR RefSeq; WP_011726638.1; NZ_SIJM01000058.1.
DR RefSeq; YP_884478.1; NC_008596.1.
DR PDB; 5CYU; X-ray; 3.07 A; A=73-479.
DR PDBsum; 5CYU; -.
DR AlphaFoldDB; A0QNJ0; -.
DR SMR; A0QNJ0; -.
DR STRING; 246196.MSMEI_0061; -.
DR PRIDE; A0QNJ0; -.
DR EnsemblBacteria; ABK72695; ABK72695; MSMEG_0060.
DR EnsemblBacteria; AFP36543; AFP36543; MSMEI_0061.
DR GeneID; 66738250; -.
DR KEGG; msg:MSMEI_0061; -.
DR KEGG; msm:MSMEG_0060; -.
DR PATRIC; fig|246196.19.peg.58; -.
DR eggNOG; COG3266; Bacteria.
DR OMA; WQREPGD; -.
DR OrthoDB; 311112at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="ESX-1 secretion system ATPase EccB1"
FT /id="PRO_0000438312"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..479
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:26922638"
FT REGION 75..127
FT /note="Structural repeat A1/1"
FT /evidence="ECO:0000305|PubMed:26922638"
FT REGION 187..243
FT /note="Structural repeat C1/2"
FT /evidence="ECO:0000305|PubMed:26922638"
FT REGION 267..323
FT /note="Structural repeat A2/3"
FT /evidence="ECO:0000305|PubMed:26922638"
FT REGION 392..447
FT /note="Structural repeat C2/4"
FT /evidence="ECO:0000305|PubMed:26922638"
FT DISULFID 152..347
FT /evidence="ECO:0000269|PubMed:26922638,
FT ECO:0007744|PDB:5CYU"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:5CYU"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:5CYU"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:5CYU"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:5CYU"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:5CYU"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:5CYU"
SQ SEQUENCE 479 AA; 51022 MW; BB7F3268BF10A69B CRC64;
MAGFRLTTKV QVSGWRFLLR RVEHAIVRRD TRMFDDPLQF YSRAVFAGVV VSVLICLGAA
LMAYFKPLGK QGSDQLLVDR TTNQLYVMLP GSNQLRPVYN LTSARLVLGN ASNPVAVKSE
ELNRISKGQS IGIPGAPYAT PTGTPASQWT LCDTVAKPDS SAPKVETSIL IRTLAIDSGV
GPIRADQGML VSYEGANWLI TEGGRHSIDL ADRAVTSAVG IPVTAKPTPI SQGLFNALPN
RGPWQLPQIP AAGAPNSVGL PENLVIGSVF RTATESDPQH YVVLPDGVAR VNNTTAAALR
ATNSYGLMQP PAVEASVVAK IPEQVYVSPL PDQPLDVLLR QDSPVLCWSW QREPGDQAPK
TTVIAGRRLP LPANAIGTGI DQIGGDSTVY IEGGQFVRLQ SPDPRVGESM YYIDPQGVRY
GIANDDAAKN LGLAGPVNAP WQVVGLLVDG PVLSKEAALI EHDTLPADPN PRKVASGEG
