ECCB1_MYCTU
ID ECCB1_MYCTU Reviewed; 480 AA.
AC P9WNR7; L0TDT4; O69734; Q7D4P7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=ESX-1 secretion system ATPase EccB1 {ECO:0000305};
DE EC=3.6.-.- {ECO:0000305};
DE AltName: Full=ESX conserved component B1 {ECO:0000303|PubMed:19876390};
DE AltName: Full=Type VII secretion system protein EccB1 {ECO:0000305};
DE Short=T7SS protein EccB1 {ECO:0000305};
GN Name=eccB1 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv3869;
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 FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=16368961; DOI=10.1128/iai.74.1.88-98.2006;
RA Brodin P., Majlessi L., Marsollier L., de Jonge M.I., Bottai D.,
RA Demangel C., Hinds J., Neyrolles O., Butcher P.D., Leclerc C., Cole S.T.,
RA Brosch R.;
RT "Dissection of ESAT-6 system 1 of Mycobacterium tuberculosis and impact on
RT immunogenicity and virulence.";
RL Infect. Immun. 74:88-98(2006).
RN [3]
RP NOMENCLATURE, AND SUBUNIT.
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 [4]
RP SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19854905; DOI=10.1128/jb.01032-09;
RA Callahan B., Nguyen K., Collins A., Valdes K., Caplow M., Crossman D.K.,
RA Steyn A.J., Eisele L., Derbyshire K.M.;
RT "Conservation of structure and protein-protein interactions mediated by the
RT secreted mycobacterial proteins EsxA, EsxB, and EspA.";
RL J. Bacteriol. 192:326-335(2010).
RN [5]
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 [6] {ECO:0007744|PDB:3X3M, ECO:0007744|PDB:3X3N}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-480, FUNCTION AS AN ATPASE,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY, ATP-BINDING, DISULFIDE BOND, AND
RP MUTAGENESIS OF 72-GLY--LEU-105; ARG-102; CYS-150; 449-PRO--PRO-480 AND
RP 463-LEU--PRO-480.
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).
RN [7] {ECO:0007744|PDB:5EBC, ECO:0007744|PDB:5EBD}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 72-480.
RC STRAIN=H37Rv;
RX PubMed=26841765; DOI=10.1107/s2053230x16000212;
RA Xie X.Q., Zhang X.L., Qi C., Li D.F., Fleming J., Wang D.C., Bi L.J.;
RT "Crystallographic observation of the movement of the membrane-distal domain
RT of the T7SS core component EccB1 from Mycobacterium tuberculosis.";
RL Acta Crystallogr. F Struct. Biol. Commun. 72:139-144(2016).
RN [8] {ECO:0007744|PDB:4KK7}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 72-463, DOMAIN, TOPOLOGY, AND
RP DISULFIDE BOND.
RC STRAIN=H37Rv;
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 (PubMed:26396239). Part of the ESX-1 specialized
CC secretion system, which delivers several virulence factors to host
CC cells during infection, including the key virulence factors EsxA (ESAT-
CC 6) and EsxB (CFP-10) (PubMed:16368961). {ECO:0000269|PubMed:16368961,
CC ECO:0000269|PubMed:26396239}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:26396239};
CC Note=Ca(2+) has 50% activity (PubMed:26396239).
CC {ECO:0000269|PubMed:26396239};
CC -!- ACTIVITY REGULATION: ATPase activity inhibited by EDTA
CC (PubMed:26396239). {ECO:0000269|PubMed:26396239}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=94.94 uM for ATP, whole protein {ECO:0000269|PubMed:26396239};
CC KM=9.87 uM for ATP, residues 72-480 {ECO:0000269|PubMed:26396239};
CC Note=kcat is 0.76 min (-1) for full-length protein, kcat is 0.11 min
CC (-1) for residues 72-480. {ECO:0000269|PubMed:26396239};
CC -!- SUBUNIT: Oligomerizes, possibly a hexamer (PubMed:26396239). Part of
CC the ESX-1 / type VII secretion system (T7SS), which is composed of
CC cytosolic and membrane components. The ESX-1 membrane complex is
CC composed of EccB1, EccCa1, EccCb1, EccD1 and EccE1. Residues 72-342
CC interact with an artificial EsxB-EsxA heterodimer (PubMed:19854905).
CC {ECO:0000269|PubMed:16368961, ECO:0000269|PubMed:19854905,
CC ECO:0000305|PubMed:19876390, ECO:0000305|PubMed:26396239}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:26396239}; Single-pass membrane protein
CC {ECO:0000255}. Note=Resides at or near the cell wall, the protein is
CC susceptible to extracellular proteases (PubMed:26396239).
CC {ECO:0000269|PubMed:26396239}.
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:26396239, PubMed:26841765, PubMed:26922638). Repeat A2
CC (approximately residues 265-323) is farthest from the cell inner
CC membrane and is quite mobile, swinging on 2 inter-repeat loops (A,
CC residues 234-264 and B, 324-341) (PubMed:26841765).
CC {ECO:0000269|PubMed:26396239, ECO:0000269|PubMed:26841765,
CC ECO:0000269|PubMed:26922638}.
CC -!- DISRUPTION PHENOTYPE: Disruption abolishes EsxA and EsxB secretion, but
CC not their expression. It results in a lack of antigen specific
CC immunogenicity and leads to attenuated virulence.
CC {ECO:0000269|PubMed:16368961}.
CC -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46698.1; -; Genomic_DNA.
DR PIR; C70802; C70802.
DR RefSeq; NP_218386.1; NC_000962.3.
DR RefSeq; WP_003399854.1; NZ_NVQJ01000074.1.
DR PDB; 3X3M; X-ray; 1.90 A; A=72-480.
DR PDB; 3X3N; X-ray; 2.00 A; A=72-480.
DR PDB; 4KK7; X-ray; 1.68 A; A=72-463.
DR PDB; 5EBC; X-ray; 3.00 A; A=72-480.
DR PDB; 5EBD; X-ray; 2.60 A; A=72-480.
DR PDBsum; 3X3M; -.
DR PDBsum; 3X3N; -.
DR PDBsum; 4KK7; -.
DR PDBsum; 5EBC; -.
DR PDBsum; 5EBD; -.
DR AlphaFoldDB; P9WNR7; -.
DR SMR; P9WNR7; -.
DR IntAct; P9WNR7; 1.
DR STRING; 83332.Rv3869; -.
DR PaxDb; P9WNR7; -.
DR DNASU; 886166; -.
DR GeneID; 886166; -.
DR KEGG; mtu:Rv3869; -.
DR TubercuList; Rv3869; -.
DR eggNOG; COG3266; Bacteria.
DR OMA; WQREPGD; -.
DR PhylomeDB; P9WNR7; -.
DR SABIO-RK; P9WNR7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0052553; P:modulation by symbiont of host immune response; IDA:MTBBASE.
DR DisProt; DP01739; -.
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..480
FT /note="ESX-1 secretion system ATPase EccB1"
FT /id="PRO_0000393228"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..480
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:26396239,
FT ECO:0000305|PubMed:26922638"
FT REGION 72..135
FT /note="Structural repeat A1/1"
FT /evidence="ECO:0000305|PubMed:26396239,
FT ECO:0000305|PubMed:26841765, ECO:0000305|PubMed:26922638"
FT REGION 181..242
FT /note="Structural repeat C1/2"
FT /evidence="ECO:0000305|PubMed:26396239,
FT ECO:0000305|PubMed:26841765, ECO:0000305|PubMed:26922638"
FT REGION 243..264
FT /note="Loop A"
FT /evidence="ECO:0000305|PubMed:26841765"
FT REGION 265..323
FT /note="Structural repeat A2/3"
FT /evidence="ECO:0000305|PubMed:26396239,
FT ECO:0000305|PubMed:26841765, ECO:0000305|PubMed:26922638"
FT REGION 324..341
FT /note="Loop B"
FT /evidence="ECO:0000305|PubMed:26841765"
FT REGION 391..451
FT /note="Structural repeat C2/4"
FT /evidence="ECO:0000305|PubMed:26396239,
FT ECO:0000305|PubMed:26841765, ECO:0000305|PubMed:26922638"
FT REGION 461..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 150..345
FT /evidence="ECO:0000269|PubMed:26396239,
FT ECO:0000269|PubMed:26922638, ECO:0007744|PDB:4KK7"
FT MUTAGEN 72..105
FT /note="Missing: No ATPase activity (residues 106-480
FT only)."
FT /evidence="ECO:0000269|PubMed:26396239"
FT MUTAGEN 102
FT /note="R->A: Retains 40% ATPase activity (in residues 72-
FT 480)."
FT /evidence="ECO:0000269|PubMed:26396239"
FT MUTAGEN 150
FT /note="C->S: Retains only 20% decrease ATPase activity (in
FT residues 72-480); probably due to loss of secondary
FT structure."
FT /evidence="ECO:0000269|PubMed:26396239"
FT MUTAGEN 449..480
FT /note="Missing: 2-fold increase in ATPase activity
FT (residues 72-448 only)."
FT /evidence="ECO:0000269|PubMed:26396239"
FT MUTAGEN 463..480
FT /note="Missing: 6-fold increase in ATPase activity
FT (residues 106-463 only)."
FT /evidence="ECO:0000269|PubMed:26396239"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3X3M"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5EBC"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5EBC"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5EBD"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3X3M"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3X3N"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:5EBD"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 393..411
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:3X3M"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:3X3M"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3X3M"
SQ SEQUENCE 480 AA; 51093 MW; D19CAD0FB2B9DE4A CRC64;
MGLRLTTKVQ VSGWRFLLRR LEHAIVRRDT RMFDDPLQFY SRSIALGIVV AVLILAGAAL
LAYFKPQGKL GGTSLFTDRA TNQLYVLLSG QLHPVYNLTS ARLVLGNPAN PATVKSSELS
KLPMGQTVGI PGAPYATPVS AGSTSIWTLC DTVARADSTS PVVQTAVIAM PLEIDASIDP
LQSHEAVLVS YQGETWIVTT KGRHAIDLTD RALTSSMGIP VTARPTPISE GMFNALPDMG
PWQLPPIPAA GAPNSLGLPD DLVIGSVFQI HTDKGPQYYV VLPDGIAQVN ATTAAALRAT
QAHGLVAPPA MVPSLVVRIA ERVYPSPLPD EPLKIVSRPQ DPALCWSWQR SAGDQSPQST
VLSGRHLPIS PSAMNMGIKQ IHGTATVYLD GGKFVALQSP DPRYTESMYY IDPQGVRYGV
PNAETAKSLG LSSPQNAPWE IVRLLVDGPV LSKDAALLEH DTLPADPSPR KVPAGASGAP
