ID   ESSC_STAAM              Reviewed;        1479 AA.
AC   Q932J9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Type VII secretion system protein EssC {ECO:0000305};
GN   Name=essC {ECO:0000303|PubMed:17680693}; OrderedLocusNames=SAV0287;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2] {ECO:0007744|PDB:1WV3}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-230, AND DOMAIN.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=17680693; DOI=10.1002/prot.21302;
RA   Tanaka Y., Kuroda M., Yasutake Y., Yao M., Tsumoto K., Watanabe N.,
RA   Ohta T., Tanaka I.;
RT   "Crystal structure analysis reveals a novel forkhead-associated domain of
RT   ESAT-6 secretion system C protein in Staphylococcus aureus.";
RL   Proteins 69:659-664(2007).
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   -!- DOMAIN: The N-terminal region is composed of two iterations of
CC       forkhead-associated (FHA) domain-like structures, which could interact
CC       with other proteins in the Esx secretion system.
CC       {ECO:0000269|PubMed:17680693}.
CC   -!- SIMILARITY: Belongs to the EssC family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB56449.2; -; Genomic_DNA.
DR   RefSeq; WP_000549287.1; NC_002758.2.
DR   PDB; 1WV3; X-ray; 1.75 A; A=1-230.
DR   PDBsum; 1WV3; -.
DR   AlphaFoldDB; Q932J9; -.
DR   SMR; Q932J9; -.
DR   TCDB; 3.A.7.17.1; the type iv (conjugal dna-protein transfer or virb) secretory pathway (ivsp) family.
DR   PaxDb; Q932J9; -.
DR   EnsemblBacteria; BAB56449; BAB56449; SAV0287.
DR   KEGG; sav:SAV0287; -.
DR   HOGENOM; CLU_003134_2_1_9; -.
DR   OMA; WEWMKWL; -.
DR   PhylomeDB; Q932J9; -.
DR   BioCyc; SAUR158878:SAV_RS01615-MON; -.
DR   Proteomes; UP000002481; 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   3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Repeat; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..1479
FT                   /note="Type VII secretion system protein EssC"
FT                   /id="PRO_0000098330"
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;  170932 MW;  DD349832D2A63564 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 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 DKIAKAIRIF
     NDEIDRRKKI LSQYRVTSIS EYRKLTGETI PYVFILIDNF DAVKDSPFQE VFENMMIKMT
     REGLALDMQV TLTASRANAM KTPMYINMKT RIAMFLYDKS EVSNVVGQQK FAVKDVVGRA
     LLSSDDNVSF HIGQPFKHDE TKSYNDQIND EVSAMTEFYK GETPNDIPMM PDEIKYEDYR
     ESLSLPDIVA NGALPIGLDY EGVTLQKIKL TEPAMISSEN PREIAHIAEI MMKEIDILNE
     KYAICIADSS GEFKAYRHQV ANFAEEREDI KAIHQLMIED LKQREMDGPF EKDSLYIIND
     FKTYIDCTYI PEDDVKKLIT KGPELGLNIL FVGIHKELID AYDKQIDVAR KMINQFSIGI
     RISDQQFFKF RFIQREPVIK ENEAYMVANQ AYQKIRWFK