ESSB_STAAE
ID ESSB_STAAE Reviewed; 444 AA.
AC P0C053; A0A0H3K6K4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Type VII secretion system protein EssB {ECO:0000305};
GN Name=essB {ECO:0000303|PubMed:15657139};
GN OrderedLocusNames=NWMN_0222 {ECO:0000312|EMBL:BAF66494.1};
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Newman;
RX PubMed=15657139; DOI=10.1073/pnas.0405620102;
RA Burts M.L., Williams W.A., DeBord K., Missiakas D.M.;
RT "EsxA and EsxB are secreted by an ESAT-6-like system that is required for
RT the pathogenesis of Staphylococcus aureus infections.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1169-1174(2005).
CC -!- FUNCTION: Component of the type VII secretion system (Ess) (Probable).
CC Required for the secretion of EsxA and EsxB (PubMed:15657139).
CC {ECO:0000269|PubMed:15657139, ECO:0000305}.
CC -!- INTERACTION:
CC P0C053; P0C053: essB; NbExp=2; IntAct=EBI-11666617, EBI-11666617;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2G185};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutations abolish synthesis and secretion of both
CC EsxA and EsxB, without affecting their transcription.
CC {ECO:0000269|PubMed:15657139}.
CC -!- SIMILARITY: Belongs to the EssB family. {ECO:0000305}.
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DR EMBL; AP009351; BAF66494.1; -; Genomic_DNA.
DR RefSeq; WP_000240338.1; NZ_CP023390.1.
DR AlphaFoldDB; P0C053; -.
DR SMR; P0C053; -.
DR MINT; P0C053; -.
DR PRIDE; P0C053; -.
DR EnsemblBacteria; BAF66494; BAF66494; NWMN_0222.
DR KEGG; sae:NWMN_0222; -.
DR HOGENOM; CLU_049737_0_0_9; -.
DR OMA; FLHYGVK; -.
DR PHI-base; PHI:6220; -.
DR Proteomes; UP000006386; 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:0042802; F:identical protein binding; IPI:IntAct.
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_0000087067"
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