ID   ECCB2_MYCTO             Reviewed;         495 AA.
AC   P9WNR4; L0TE37; O05449; Q7D4N1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=ESX-2 secretion system ATPase EccB2;
DE            EC=3.6.-.- {ECO:0000305};
DE   AltName: Full=ESX conserved component B2;
DE   AltName: Full=Type VII secretion system protein EccB2;
DE            Short=T7SS protein EccB2;
GN   Name=eccB2; OrderedLocusNames=MT4011;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: An ATPase (By similarity). {ECO:0000250|UniProtKB:P9WNR7}.
CC   -!- SUBUNIT: Part of the ESX-2 / type VII secretion system (T7SS), which is
CC       composed of cytosolic and membrane components.
CC       {ECO:0000250|UniProtKB:P9WNR7}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48377.1; -; Genomic_DNA.
DR   PIR; H70598; H70598.
DR   RefSeq; WP_003400065.1; NZ_KK341228.1.
DR   AlphaFoldDB; P9WNR4; -.
DR   SMR; P9WNR4; -.
DR   EnsemblBacteria; AAK48377; AAK48377; MT4011.
DR   KEGG; mtc:MT4011; -.
DR   PATRIC; fig|83331.31.peg.4318; -.
DR   HOGENOM; CLU_036302_3_0_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="ESX-2 secretion system ATPase EccB2"
FT                   /id="PRO_0000427081"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  51587 MW;  24C0C414C7C1C2B5 CRC64;
     MPLSLSNRDQ NSGHLFYNRR LRAATTRFSV RMKHDDRKQT AALALSMVLV AIAAGWMMLL
     NVLKPTGIVG DSAIIGDRDS GALYARIDGR LYPALNLTSA RLATGTAGQP TWVKPAEIAK
     YPTGPLVGIP GAPAAMPVNR GAVSAWAVCD TAGRPRSADK PVVTSIAGPI TGGGRATHLR
     DDAGLLVTFD GSTYVIWGGK RSQIDPTNRA VTLSLGLDPG VTSPIQISRA LFDGLPATEP
     LRVPAVPEAG TPSTWVPGAR VGSVLQAQTA GGGSQFYVLL PDGVQKISSF VADLLRSANS
     YGAAAPRVVT PDVLVHTPQV TSLPVEYYPA GRLNFVDTAA DPTTCVSWEK ASTDPQARVA
     VYNGRGLPVP PSMDSRIVRL VRDDRAPASV VATQVLVLPG AANFVTSTSG VITAESRESL
     FWVSGNGVRF GIANDEATLR ALGLDPGAAV QAPWPLLRTF AAGPALSRDA ALLARDTVPT
     LGQVAIVTTT AKAGA