ESSC_STAAR
ID ESSC_STAAR Reviewed; 1482 AA.
AC Q6GK24;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Type VII secretion system protein EssC {ECO:0000250|UniProtKB:P0C048};
GN Name=essC {ECO:0000250|UniProtKB:P0C048}; OrderedLocusNames=SAR0284;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Component of the type VII secretion system (Ess). Required
CC for the secretion of substrates including EsxA and EsxB. However,
CC unable to support secretion of the substrate protein EsxC.
CC {ECO:0000250|UniProtKB:Q2G184}.
CC -!- SUBUNIT: Homooligomer. Interacts with EsaE.
CC {ECO:0000250|UniProtKB:Q2G184}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2G184};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: This strain lacks esxB and esxC. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EssC family. {ECO:0000305}.
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DR EMBL; BX571856; CAG39311.1; -; Genomic_DNA.
DR RefSeq; WP_000549309.1; NC_002952.2.
DR AlphaFoldDB; Q6GK24; -.
DR SMR; Q6GK24; -.
DR KEGG; sar:SAR0284; -.
DR HOGENOM; CLU_003134_2_1_9; -.
DR OMA; WEWMKWL; -.
DR OrthoDB; 7548at2; -.
DR Proteomes; UP000000596; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..1482
FT /note="Type VII secretion system protein EssC"
FT /id="PRO_0000098332"
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..1482
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 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 1482 AA; 170971 MW; FF878C6DAD6CE5FD CRC64;
MHKLIIKYNK QLKMLNLRDG KTYTISEDER ADITLKSLGE VIHLEQNNQG TWQANHTSIN
KVLVRKGDLD DITLQLYTEA DYASFAYPSI QDTMTIGSNA YDDMVIQSLM NAIIIKDFQS
IQETQYVRIV 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 YHKLFKEGVA 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 DKIAKAIRKI
HDIISERKRL LSQERVVNIE QYNKETGNSI PNVFLIIDNY DTVKESPFME EYEEMMSKVT
REGLALGVYI ILSGSRSSAI KSAIFTNIKT RVALYLFENN ELTNIIGSYK KGVKDVKGRA
AINDDNFTQF QIAQPFELAE GQTYNERIKN EVAQMKEFYV GDYPKHIPMM PDKVFMEDIR
EAYDLEKIIH EEHKLPLGLD FEDVELVSLD LTSSSIVTAI KPTEMEKMND VIMSSLSVYS
KNQFVILVDA EDNMSQYSED VTSYYSAPSD LSNIRLGFKQ EIEARKNGEK SIEECKIVFI
NNIKRFNQLT GMTEDEIRVL FNEGQKVNII IIASGLYSDT IGAFDRESKM MVRTINQALI
SHKISEQEFI RVKDRFGEPE LKVGEMYYIN NQEYQKIKLM EG
