ID   ECCB4_MYCTO             Reviewed;         470 AA.
AC   P9WNR0; L0TE61; O06317; Q7D5I7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=ESX-4 secretion system ATPase EccB4;
DE            EC=3.6.-.- {ECO:0000305};
DE   AltName: Full=ESX conserved component B4;
DE   AltName: Full=Type VII secretion system protein EccB4;
DE            Short=T7SS protein EccB4;
GN   Name=eccB4; OrderedLocusNames=MT3556;
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-4 / 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK47896.1; -; Genomic_DNA.
DR   PIR; G70564; G70564.
DR   RefSeq; WP_003418333.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNR0; -.
DR   SMR; P9WNR0; -.
DR   EnsemblBacteria; AAK47896; AAK47896; MT3556.
DR   KEGG; mtc:MT3556; -.
DR   PATRIC; fig|83331.31.peg.3815; -.
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..470
FT                   /note="ESX-4 secretion system ATPase EccB4"
FT                   /id="PRO_0000427083"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   470 AA;  48199 MW;  61833F78B676F584 CRC64;
     MPSPATTWLH VSGYRFLLRR IECALLFGDV CAATGALRAR TTSLALGCVL AIVAAMGCAF
     VALLRPQSAL GQAPIVMGRE SGALYVRVDD VWHPVLNLAS ARLIAATNAN PQPVSESELG
     HTKRGPLLGI PGAPQLLDQP LAGAESAWAI CDSDNGGSTT VVVGPAEDSS AQVLTAEQMI
     LVATESGSPT YLLYGGRRAV VDLADPAVVW ALRLQGRVPH VVAQSLLNAV PEAPRITAPR
     IRGGGRASVG LPGFLVGGVV RITRASGDEY YVVLEDGVQR IGQVAADLLR FGDSQGSVNV
     PTVAPDVIRV APIVNTLPVS AFPDRPPTPV DGSPGRAVTT LCVTWTPAQP GAARVAFLAG
     SGPPVPLGGV PVTLAQADGR GPALDAVYLP PGRSAYVAAR SLSGGGTGTR YLVTDTGVRF
     AIHDDDVAHD LGLPTAAIPA PWPVLATLPS GPELSRANAS VARDTVAPGP