ESAA_STAA3
ID ESAA_STAA3 Reviewed; 1009 AA.
AC A0A0H2XFP1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Type VII secretion system accessory factor EsaA {ECO:0000305};
GN Name=esaA {ECO:0000303|PubMed:29737367}; OrderedLocusNames=SAUSA300_0279;
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, INTERACTION WITH ESSB, AND DISRUPTION PHENOTYPE.
RC STRAIN=USA300;
RX PubMed=28874412; DOI=10.1128/jb.00482-17;
RA Aly K.A., Anderson M., Ohr R.J., Missiakas D.;
RT "Isolation of a Membrane Protein Complex for Type VII Secretion in
RT Staphylococcus aureus.";
RL J. Bacteriol. 199:0-0(2017).
RN [3]
RP FUNCTION, AND INTERACTION WITH ESSB.
RC STRAIN=USA300;
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). Provides
CC together with EssB and other components such as EssC and EssE a
CC secretion plateform accross the cytoplasmic membrane in the host.
CC {ECO:0000269|PubMed:28874412, ECO:0000269|PubMed:29737367}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with EssB
CC (PubMed:29737367, PubMed:28874412). {ECO:0000250|UniProtKB:Q2G188,
CC ECO:0000269|PubMed:28874412, ECO:0000269|PubMed:29737367}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2G188};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion abrogates the secretion of EsxA and EsxC
CC into the extracellular medium. {ECO:0000269|PubMed:28874412}.
CC -!- SIMILARITY: Belongs to the EsaA family. {ECO:0000305}.
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DR EMBL; CP000255; ABD21191.1; -; Genomic_DNA.
DR RefSeq; WP_000728949.1; NZ_CP027476.1.
DR AlphaFoldDB; A0A0H2XFP1; -.
DR SMR; A0A0H2XFP1; -.
DR EnsemblBacteria; ABD21191; ABD21191; SAUSA300_0279.
DR KEGG; saa:SAUSA300_0279; -.
DR HOGENOM; CLU_015018_0_0_9; -.
DR OMA; MYNFYKP; -.
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 InterPro; IPR023838; T7SS_EsaA.
DR TIGRFAMs; TIGR03929; T7_esaA_Nterm; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Membrane; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..1009
FT /note="Type VII secretion system accessory factor EsaA"
FT /id="PRO_0000448088"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 680..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 114826 MW; 2F9328179F8A1792 CRC64;
MKKKNWIYAL IVTLIIIIAI VSMIFFVQTK YGDQSEKGSQ SVSNKNNKIH IAIVNEDQPT
TYNGKKVELG QAFIKRLANE KNYKFETVTR NVAESGLKNG GYQVMIVIPE NFSKLAMQLD
AKTPSKISLQ YKTAVGQKEE VAKNTEKVVS NVLNDFNKNL VEIYLTSIID NLHNAQKNVG
AIMTREHGVN SKFSNYLLNP INDFPELFTD TLVNSISANK DITKWFQTYN KSLLSANSDT
FRVNTDYNVS TLIEKQNSLF DEHNTAMDKM LQDYKSQKDS VELDNYINAL KQMDSQIDQQ
SSMQDTGKEE YKQTVKENLD KLREIIQSQE SPFSKGMIED YRKQLTESLQ DELANNKDLQ
DALNSIKMNN AQFAENLEKQ LHDDIVKEPD TDTTFIYNMS KQDFIAAGLN EDEANKYEAI
VKEAKRYKNE YNLKKPLAEH INLTDYDNQV AQDTSSLIND GVKVQRTETI KSNDINQLTV
ATDPHFNFEG DIKINGKKYD IKDQSVQLDT SNKEYKVEVN GVAKLKKDAE KDFLKDKTMH
LQLLFGQANR QDEPNDKKAT SVVDVTLNHN LDGRLSKDAL SQQLSALSRF DAHYKMYTDT
KGREDKPFDN KRLIDMMVDQ VINDMESFKD DKVAVLHQID SMEENSDKLI DDILNNKKNT
TKNKEDISKL IDQLENVKKT FAEEPQEPKI DKGKNDEFNT MSSNLDKEIS RISEKSTQLL
SDTQESKSIA DSVSGQLNQV DNNVNKLHAT GRALGVRAND LNRQMAKNDK DNELFAKEFK
KVLQNSKDGD RQNQALKAFM SNPVQKKNLE NVLANNGNTD VISPTLFVLL MYLLSMITAY
IFYSYERAKG QMNFIKDDYS SKNHLWNNVI TSGVIGTTGL VEGLIVGLIA MNKFHVLAGY
RAKFILMVIL TMMVFVLINT YLLRQVKSIG MFLMIAALGL YFVAMNNLKA AGQGVTNKIS
PLSYIDNMFF NYLNAEHPIG LVLVILTVLV IIGFVLNMFI KHFKKERLI