ID   ESPB_MYCMM              Reviewed;         454 AA.
AC   B2HNQ9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=ESX-1 secretion-associated protein EspB {ECO:0000250|UniProtKB:P9WJD9};
GN   Name=espB {ECO:0000250|UniProtKB:P9WJD9}; OrderedLocusNames=MMAR_5457;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, DOMAIN,
RP   CLEAVAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=17908204; DOI=10.1111/j.1365-2958.2007.05959.x;
RA   Xu J., Laine O., Masciocchi M., Manoranjan J., Smith J., Du S.J.,
RA   Edwards N., Zhu X., Fenselau C., Gao L.Y.;
RT   "A unique Mycobacterium ESX-1 protein co-secretes with CFP-10/ESAT-6 and is
RT   necessary for inhibiting phagosome maturation.";
RL   Mol. Microbiol. 66:787-800(2007).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17908204}.
CC       Note=Secreted via the ESX-1 / type VII secretion system (T7SS).
CC       {ECO:0000269|PubMed:17908204}.
CC   -!- DOMAIN: The C-terminus is necessary for the co-dependent secretion, for
CC       maintaining the EsxA (ESAT-6) cellular levels, and for interacting with
CC       EsxA. {ECO:0000269|PubMed:17908204}.
CC   -!- PTM: Cleaved at close to the C-terminus during secretion.
CC       {ECO:0000269|PubMed:17908204}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is extremely defective in intracellular
CC       growth. {ECO:0000269|PubMed:17908204}.
CC   -!- MISCELLANEOUS: Secretion of EspB, EsxA and EsxB is mutually dependent.
CC       {ECO:0000269|PubMed:17908204}.
CC   -!- SIMILARITY: Belongs to the EspB family. {ECO:0000305}.
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DR   EMBL; CP000854; ACC43864.1; -; Genomic_DNA.
DR   RefSeq; WP_012396956.1; NC_010612.1.
DR   AlphaFoldDB; B2HNQ9; -.
DR   SMR; B2HNQ9; -.
DR   STRING; 216594.MMAR_5457; -.
DR   EnsemblBacteria; ACC43864; ACC43864; MMAR_5457.
DR   KEGG; mmi:MMAR_5457; -.
DR   eggNOG; ENOG50341Q7; Bacteria.
DR   HOGENOM; CLU_039721_0_0_11; -.
DR   OrthoDB; 1128346at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.1260.20; -; 1.
DR   InterPro; IPR041275; EspB_PE.
DR   InterPro; IPR038332; PPE_sf.
DR   Pfam; PF18625; EspB_PE; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Secreted.
FT   CHAIN           1..454
FT                   /note="ESX-1 secretion-associated protein EspB"
FT                   /id="PRO_0000394201"
FT   REGION          17..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  46973 MW;  143EE18EEB23AEE3 CRC64;
     MSQPQTVTVD QQEILNRADE VEAPMATPPT DVPQAPSGLT AANNAAEQLA VSADNVRLYL
     QAGERERQRL ATSLRNAAAA YGEVEDESAT ALDNDGNGEV DAQSAGGAGA GQTESLEETP
     KVAAAGESDF TDLKTAATKL ESGDQGTSMV NFADGWNNFN LSLQRDIKRF RIFENWEGDA
     ATACEASMDQ QKEWILHMAK LSASLAKQAN FMAQLQLWAR RGHPTLADIV ELERLAKDPD
     YQEQAIKLYA EYQETSEKVL SEYNTKADLE PVNPPKPPAA IKIDPPPPAQ PQGLIPGFLM
     PPGDGSTGLA SGMTPPMIPP TGGAGGTPDV NTAELTSAGR EAASNLSKGL GVKPMSLGGG
     GGGLGGMPMG DAALAGGESV RPAAAGDIAG AGQGGGAAGR GMAGGGMGMP MGGAGQGQGG
     AKSKGAQQDE EALYTEDREW TEAVIGNRRR QDNK