ID   ESSB_STAA3              Reviewed;         444 AA.
AC   A0A0H2XG66;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Type VII secretion system protein EssB {ECO:0000305};
GN   Name=essB {ECO:0000303|PubMed:23006124};
GN   OrderedLocusNames=SAUSA300_0282 {ECO:0000312|EMBL:ABD21393.1};
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
RN   [2]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=USA300;
RX   PubMed=23006124; DOI=10.1186/1471-2180-12-219;
RA   Chen Y.H., Anderson M., Hendrickx A.P., Missiakas D.;
RT   "Characterization of EssB, a protein required for secretion of ESAT-6 like
RT   proteins in Staphylococcus aureus.";
RL   BMC Microbiol. 12:219-219(2012).
RN   [3]
RP   INTERACTION WITH ESAA.
RX   PubMed=29737367; DOI=10.1007/s00203-018-1519-x;
RA   Ahmed M.M., Aboshanab K.M., Ragab Y.M., Missiakas D.M., Aly K.A.;
RT   "The transmembrane domain of the Staphylococcus aureus ESAT-6 component
RT   EssB mediates interaction with the integral membrane protein EsaA,
RT   facilitating partially regulated secretion in a heterologous host.";
RL   Arch. Microbiol. 200:1075-1086(2018).
CC   -!- FUNCTION: Component of the type VII secretion system (Ess). Required
CC       for the secretion of EsxA and proper accumulation of EssB and EssD.
CC       {ECO:0000269|PubMed:23006124}.
CC   -!- SUBUNIT: May oligomerize and interact with other membrane components to
CC       form the Ess system (PubMed:23006124). Interacts with EsaA
CC       (PubMed:29737367). {ECO:0000269|PubMed:23006124,
CC       ECO:0000269|PubMed:29737367}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23006124};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Mutants cannot secrete EsxA. Deletion also
CC       affects the production of several Ess factors.
CC       {ECO:0000269|PubMed:23006124}.
CC   -!- SIMILARITY: Belongs to the EssB family. {ECO:0000305}.
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DR   EMBL; CP000255; ABD21393.1; -; Genomic_DNA.
DR   RefSeq; WP_000240338.1; NZ_CP027476.1.
DR   AlphaFoldDB; A0A0H2XG66; -.
DR   SMR; A0A0H2XG66; -.
DR   EnsemblBacteria; ABD21393; ABD21393; SAUSA300_0282.
DR   KEGG; saa:SAUSA300_0282; -.
DR   HOGENOM; CLU_049737_0_0_9; -.
DR   OMA; FLHYGVK; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.25.40.680; -; 1.
DR   InterPro; IPR018778; T7SS_EssB.
DR   InterPro; IPR042565; T7SS_EssB_C.
DR   Pfam; PF10140; YukC; 1.
DR   TIGRFAMs; TIGR03926; T7_EssB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Membrane; Transmembrane; Transmembrane helix;
KW   Virulence.
FT   CHAIN           1..444
FT                   /note="Type VII secretion system protein EssB"
FT                   /id="PRO_0000437413"
FT   TOPO_DOM        1..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G185"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..444
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G185"
FT   REGION          366..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          387..443
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        368..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  52024 MW;  FACCFE3353DE1F77 CRC64;
     MVKNHNPKNE MQDMLTPLDA EEAAKTKLRL DMREIPKSSI KPEHFHLMYL LEQHSPYFID
     AELTELRDSF QIHYDINDNH TPFDNIKSFT KNEKLRYLLN IKNLEEVNRT RYTFVLAPDE
     LFFTRDGLPI AKTRGLQNVV DPLPVSEAEF LTRYKALVIC AFNEKQSFDA LVEGNLELHK
     GTPFETKVIE AATLDLLTAF LDEQYQKQEQ DYSQNYAYVR KVGHTVFKWV AIGMTTLSVL
     LIAFLAFLYF SVMKHNERIE KGYQAFVKDD YTQVLNTYDD LDGKKLDKEA LYIYAKSYIQ
     TNKQGLEKDK KENLLNNVTP NSNKDYLLYW MELGQGHLDE AINIATYLDD NDITKLALIN
     KLNEIKNNGD LSNDKRSEET KKYNDKLQDI LDKEKQVKDE KAKSEEEKAK AKDEKLKQQE
     ENEKKQKEQA QKDKEKRQEA ERKK