ESSC_STAA8
ID ESSC_STAA8 Reviewed; 1479 AA.
AC Q2G184;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Type VII secretion system protein EssC {ECO:0000305};
GN Name=essC {ECO:0000303|PubMed:26785823};
GN OrderedLocusNames=SAOUHSC_00262 {ECO:0000312|EMBL:ABD29436.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=RN6390;
RX PubMed=26785823; DOI=10.1002/1873-3468.12065;
RA Jaeger F., Zoltner M., Kneuper H., Hunter W.N., Palmer T.;
RT "Membrane interactions and self-association of components of the Ess/Type
RT VII secretion system of Staphylococcus aureus.";
RL FEBS Lett. 590:349-357(2016).
RN [3]
RP POSSIBLE FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=RN6390;
RX PubMed=27130157; DOI=10.1042/bcj20160257;
RA Zoltner M., Ng W.M., Money J.J., Fyfe P.K., Kneuper H., Palmer T.,
RA Hunter W.N.;
RT "EssC: domain structures inform on the elusive translocation channel in the
RT Type VII secretion system.";
RL Biochem. J. 473:1941-1952(2016).
RN [4]
RP INTERACTION WITH ESAE, AND SUBUNIT.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=27723728; DOI=10.1038/nmicrobiol.2016.183;
RA Cao Z., Casabona M.G., Kneuper H., Chalmers J.D., Palmer T.;
RT "The type VII secretion system of Staphylococcus aureus secretes a nuclease
RT toxin that targets competitor bacteria.";
RL Nat. Microbiol. 2:16183-16183(2016).
RN [5]
RP FUNCTION.
RC STRAIN=RN6390;
RX PubMed=29620499; DOI=10.1099/mic.0.000650;
RA Jaeger F., Kneuper H., Palmer T.;
RT "EssC is a specificity determinant for Staphylococcus aureus type VII
RT secretion.";
RL Microbiology 164:816-820(2018).
CC -!- FUNCTION: Component of the type VII secretion system (Ess). Required
CC for the secretion of substrates including EsxA and EsxB
CC (PubMed:27130157, PubMed:29620499). However, unable to support
CC secretion of the substrate protein EsxC (PubMed:29620499).
CC {ECO:0000269|PubMed:27130157, ECO:0000269|PubMed:29620499}.
CC -!- SUBUNIT: Homooligomer (PubMed:26785823, PubMed:27723728). Interacts
CC with EsaE (PubMed:27723728). {ECO:0000269|PubMed:26785823,
CC ECO:0000269|PubMed:27723728}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26785823};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Loss of secretion of EsxA and EsxC but not their
CC expression (PubMed:27130157). {ECO:0000269|PubMed:27130157}.
CC -!- SIMILARITY: Belongs to the EssC family. {ECO:0000305}.
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DR EMBL; CP000253; ABD29436.1; -; Genomic_DNA.
DR RefSeq; WP_000549278.1; NZ_LS483365.1.
DR RefSeq; YP_498856.1; NC_007795.1.
DR AlphaFoldDB; Q2G184; -.
DR SMR; Q2G184; -.
DR STRING; 93061.SAOUHSC_00262; -.
DR EnsemblBacteria; ABD29436; ABD29436; SAOUHSC_00262.
DR GeneID; 3919204; -.
DR KEGG; sao:SAOUHSC_00262; -.
DR PATRIC; fig|93061.5.peg.241; -.
DR HOGENOM; CLU_003134_2_1_9; -.
DR OMA; WEWMKWL; -.
DR PRO; PR:Q2G184; -.
DR Proteomes; UP000008816; 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:0003677; F:DNA binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR023839; Firmicutes_EssC_C.
DR InterPro; IPR022206; Firmicutes_EssC_N.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR Pfam; PF12538; FtsK_SpoIIIE_N; 1.
DR SUPFAM; SSF49879; SSF49879; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03928; T7_EssCb_Firm; 1.
DR PROSITE; PS50901; FTSK; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..1479
FT /note="Type VII secretion system protein EssC"
FT /id="PRO_0000437415"
FT TOPO_DOM 1..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C048"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..256
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0C048"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..1479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C048"
FT DOMAIN 652..846
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 997..1183
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..189
FT /note="Required for substrate secretion, protein missing
FT this segment is unstable"
FT /evidence="ECO:0000269|PubMed:27130157"
FT REGION 1249..1479
FT /note="Required for substrate secretion, truncated protein
FT is stable"
FT /evidence="ECO:0000269|PubMed:27130157"
FT BINDING 672..679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 1014..1021
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1479 AA; 170931 MW; 0EC13F663848BBCB CRC64;
MHKLIIKYNK QLKMLNLRDG KTYTISEDER ADITLKSLGE VIHLEQNNQG TWQANHTSIN
KVLVRKGDLD DITLQLYTEA DYASFAYPSI QDTMTIGPNA YDDMVIQSLM NAIIIKDFQS
IQESQYVRIV HDKNTDVYIN YELQEQLTNK AYIGDHIYVE GIWLEVQADG LNVLSQNTVA
SSLIRLTQEM PHAQADDYNT YHRSPRIIHR EPTDDIKIER PPQPIQKNNT VIWRSIIPPL
VMIALTVVIF LVRPIGIYIL MMIGMSTVTI VFGITTYFSE KKKYNKDVEK REKDYKAYLD
NKSKEINKAI KAQRFSLNYH YPTVAEIKDI VETKAPRIYE KTSHHHDFLH YKLGIANVEK
SFKLDYQEEE FNQRRDELFD DAKELYEFYT DVEQAPLIND LNHGPIAYIG ARHLILEELE
KMLIQLSTFH SYHDLEFLFV TREDEVETLK WARWLPHMTL RGQNIRGFVY NQRTRDQILT
SIYSMIKERI QAVRERSRSN EQIIFTPQLV FVITDMSLII DHVILEYVNQ DLSEYGISLI
FVEDVIESLP EHVDTIIDIK SRTEGELITK EKELVQLKFT PENIDNVDKE YIARRLANLI
HVEHLKNAIP DSITFLEMYN VKEVDQLDVV NRWRQNETYK TMAVPLGVRG KDDILSLNLH
EKAHGPHGLV AGTTGSGKSE IIQSYILSLA INFHPHEVAF LLIDYKGGGM ANLFKDLVHL
VGTITNLDGD EAMRALTSIK AELRKRQRLF GEHDVNHINQ YHKLFKEGIA TEPMPHLFII
SDEFAELKSE QPDFMKELVS TARIGRSLGI HLILATQKPS GVVDDQIWSN SKFKLALKVQ
DRQDSNEILK TPDAADITLP GRAYLQVGNN EIYELFQSAW SGATYDIEGD KLEVEDKTIY
MINDYGQLQA INKDLSGLED EETKENQTEL EAVIDHIESI TTRLEIEEVK RPWLPPLPEN
VYQEDLVETD FRKLWSDDAK EVELTLGLKD VPEEQYQGPM VLQLKKAGHI ALIGSPGYGR
TTFLHNIIFD VARHHRPDQA HMYLFDFGTN GLMPVTDIPH VADYFTVDQE DKIAKAIRIF
NDEIDRRKKI LSQYRVTSIS EYRKLTGETI PHVFILIDNF DAVKDSPFQE VFENMMIKMT
REGLALDMQV TLTASRANAM KTPMYINMKT RIAMFLYDKS EVSNVVGQQK FAVKDVVGRA
LLSSDDNVSF HIGQPFKHDE TKSYNDQIND EVSAMTEFYK GETPNDIPMM PDEIKYEDYR
ESLNLPDIVA NGALPIGLDY EGVTLQKIKL TEPAMISSEN PREIAHIAEI MMKEIDILNE
KYAICIADSS GEFKAYRHQV ANFAEEREDI KAIHQLMIED LKQREMDGPF EKDSLYIIND
FKTFIDCTYI PEDDVKKLIT KGPELGLNIL FVGIHKELID AYDKQIDVAR KMINQFSIGI
RISDQQFFKF RFIQREPVIK ENEAYMVANQ AYQKIRWFK
