ESSC_STAAS
ID ESSC_STAAS Reviewed; 1479 AA.
AC Q6GCI5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Type VII secretion system protein EssC {ECO:0000250|UniProtKB:P0C048};
GN Name=essC {ECO:0000250|UniProtKB:P0C048}; OrderedLocusNames=SAS0263;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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 -!- SIMILARITY: Belongs to the EssC family. {ECO:0000305}.
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DR EMBL; BX571857; CAG42034.1; -; Genomic_DNA.
DR RefSeq; WP_000549274.1; NC_002953.3.
DR AlphaFoldDB; Q6GCI5; -.
DR SMR; Q6GCI5; -.
DR KEGG; sas:SAS0263; -.
DR HOGENOM; CLU_003134_2_1_9; -.
DR OMA; WEWMKWL; -.
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..1479
FT /note="Type VII secretion system protein EssC"
FT /id="PRO_0000098333"
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 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; 170891 MW; 96A9A5BB1471B634 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 MMIGMSSVTI VFGITTYFSE KKKYNKDVEK REKDYKDYLD
NKSKEINKAI KAQRFSLNYH YPTVAEIKDI VETKAPRIYE KTSHHHDFLH YKLGIANVEK
SFKLDYQEEE FNQRRDELFD DAKELYEFYT DVEQAPLIND LNHGPIAYIG ARHLILEELE
KMLIQLSIFH SYHDLEFLFV TREDEVETLK WARWLPHMTL RGQNIRGFVY NQRTRDQILT
SIYSMIKERI QAVRERSKSN 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 GETPSDIPMM PDEIKYEDYR
ESLSLPDIVA NGALPIGLDY EGVTLQKIKL TEPAMISSEN PREIAHIAEI MMKEIDILNE
KYAICIADSS GEFKAYRHQV ANFAEEREDI KAIHQLMIED LKQREMDGPF EKDSLYIIND
FKTFIDCTYI PEDDVKKLIT KGPELGLNIL FVGIHKELID AYDKQIDVAR KMINQFSIGI
RISDQQFFKF RFIQREPVIK ENEAYMVANQ AYQKIRWFK
