ECCC_THECD
ID ECCC_THECD Reviewed; 1315 AA.
AC D1A4G7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ESX secretion system protein EccC {ECO:0000303|PubMed:25865481};
DE AltName: Full=Type VII secretion system protein EccC {ECO:0000305};
DE Short=T7SS protein EccC {ECO:0000305};
GN Name=eccC {ECO:0000303|PubMed:25865481}; OrderedLocusNames=Tcur_0607;
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC Thermomonospora.
OX NCBI_TaxID=471852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goeker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
RN [2] {ECO:0007744|PDB:4N1A, ECO:0007744|PDB:4NH0}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 200-1315 IN COMPLEX WITH ATP,
RP X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) OF 759-1315 IN COMPLEX WITH ESXB
RP C-TERMINUS AND ATP, ELECTRON MICROSCOPY, FUNCTION, ACTIVITY REGULATION,
RP PROBABLE ACTIVE SITE, INTERACTION WITH ESXB, SUBUNIT, DOMAIN, PROBABLE
RP TOPOLOGY, AND MUTAGENESIS OF ARG-543; GLU-593; ARG-616; ARG-892; ILE-1163;
RP ILE-1179 AND LEU-1208.
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=25865481; DOI=10.1016/j.cell.2015.03.040;
RA Rosenberg O.S., Dovala D., Li X., Connolly L., Bendebury A.,
RA Finer-Moore J., Holton J., Cheng Y., Stroud R.M., Cox J.S.;
RT "Substrates control multimerization and activation of the multi-domain
RT ATPase motor of type VII secretion.";
RL Cell 161:501-512(2015).
CC -!- FUNCTION: Part of the ESX specialized secretion system, which exports
CC proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10)
CC (PubMed:25865481). Has weak intrinsic ATPase activity; probably only
CC the first FtsK domain can hydrolyze ATP (PubMed:25865481). Might be the
CC translocase subunit (PubMed:25865481). {ECO:0000269|PubMed:25865481}.
CC -!- ACTIVITY REGULATION: EsxB binding to the third FtsK domain causes
CC multimerization; a subsequent unknown step relieves the allosteric
CC inhibition of linker 2 on FtsK domain 1, activating the ATPase
CC activity; a mutant EsxB ('Ala-98') does not cause multimers to form
CC (PubMed:25865481). {ECO:0000269|PubMed:25865481}.
CC -!- SUBUNIT: The cytosolic domain can form homodimers (PubMed:25865481).
CC Binds EsxB, which leads to multimerization, however EsxA disassembles
CC the multimers, possibly by making EccC-EsxA-EsxB trimers instead of
CC EccC-EsxB-EsxB-EccC tetramers. Forms a complex with EsxA and EsxB,
CC probably wholly mediated by EsxB (PubMed:25865481).
CC {ECO:0000269|PubMed:25865481}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The cytoplasmic domain is a rigid structure with 4 domains
CC (residues 276 to 401 form an unnamed domain) plus the 3 FtsK (ATPase)
CC domains which are connected by short linkers. Binds EsxB via a small
CC pocket (residues 1163-1208) in the third FtsK (ATPase) domain; the
CC linkers between FtsK 1-2 and FtsK 2-3 bind in an analogous manner to
CC FtsK 1 and FtsK 2. Linker 2 binding to FtsK 1 decreases its ATPase
CC activity and probably controls it (PubMed:25865481).
CC {ECO:0000269|PubMed:25865481}.
CC -!- MISCELLANEOUS: Unlike the well characterized M.tuberculosis ESX-1
CC cluster, this protein is not split into 2 genes. This subunit and a
CC WGX100 family protein are the only proteins universally associated with
CC T7SS. {ECO:0000305|PubMed:25865481}.
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DR EMBL; CP001738; ACY96202.1; -; Genomic_DNA.
DR RefSeq; WP_012850986.1; NC_013510.1.
DR PDB; 4N1A; X-ray; 3.24 A; A/B/C/E=759-1315.
DR PDB; 4NH0; X-ray; 2.90 A; A/B=200-1315.
DR PDBsum; 4N1A; -.
DR PDBsum; 4NH0; -.
DR AlphaFoldDB; D1A4G7; -.
DR SMR; D1A4G7; -.
DR STRING; 471852.Tcur_0607; -.
DR EnsemblBacteria; ACY96202; ACY96202; Tcur_0607.
DR KEGG; tcu:Tcur_0607; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_003134_1_0_11; -.
DR OMA; PNTSAMW; -.
DR OrthoDB; 7548at2; -.
DR Proteomes; UP000001918; 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 DisProt; DP02490; -.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR023836; EccCa-like_Actinobacteria.
DR InterPro; IPR023837; EccCb-like_Actinobacteria.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01580; FtsK_SpoIIIE; 3.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 3.
DR TIGRFAMs; TIGR03924; T7SS_EccC_a; 1.
DR TIGRFAMs; TIGR03925; T7SS_EccC_b; 1.
DR PROSITE; PS50901; FTSK; 3.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1315
FT /note="ESX secretion system protein EccC"
FT /id="PRO_0000438309"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..64
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..1315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25865481"
FT DOMAIN 456..656
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 813..1004
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 1099..1282
FT /note="FtsK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..1315
FT /note="Binds EsxB"
FT /evidence="ECO:0000269|PubMed:25865481"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 593
FT /evidence="ECO:0000305|PubMed:25865481"
FT BINDING 479..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 834..839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289,
FT ECO:0007744|PDB:4N1A, ECO:0007744|PDB:4NH0"
FT BINDING 1031
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4N1A, ECO:0007744|PDB:4NH0"
FT BINDING 1119..1124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289,
FT ECO:0007744|PDB:4N1A, ECO:0007744|PDB:4NH0"
FT BINDING 1293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:4N1A, ECO:0007744|PDB:4NH0"
FT BINDING 1310..1311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:4N1A, ECO:0007744|PDB:4NH0"
FT MUTAGEN 543
FT /note="R->A: Increased intrinsic ATPase activity; ATPase is
FT activated by wild-type but not mutant EsxB A-98."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 593
FT /note="E->Q: No longer activates ATPase; when associated
FT with A-543."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 616
FT /note="R->Q: Increased intrinsic ATPase activity without
FT concentration-dependency; when associated with A-543."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 892
FT /note="R->A: No change in intrinsic ATPase activity."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 1163
FT /note="I->T: No longer interacts with EsxB."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 1179
FT /note="I->N: No longer interacts with EsxB."
FT /evidence="ECO:0000269|PubMed:25865481"
FT MUTAGEN 1208
FT /note="L->T: No longer interacts with EsxB."
FT /evidence="ECO:0000269|PubMed:25865481"
FT TURN 772..775
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 793..796
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 797..806
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 814..819
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 826..830
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 837..850
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 854..856
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 868..872
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 878..882
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 887..910
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 916..923
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 924..926
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 935..941
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 943..949
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 951..963
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 965..967
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 969..974
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 978..980
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 983..986
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 991..996
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1000..1002
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1007..1011
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1020..1022
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1028..1031
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1045..1059
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1073..1076
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 1077..1079
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1083..1086
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1090..1095
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 1096..1098
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1101..1104
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 1106..1108
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1112..1116
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1122..1136
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 1139..1141
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1142..1147
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1154..1156
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1157..1159
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1162..1166
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1169..1184
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1194..1199
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1207..1213
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1215..1217
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1226..1234
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1235..1238
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1240..1246
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1253..1255
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1258..1265
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1270..1274
FT /evidence="ECO:0007829|PDB:4N1A"
FT HELIX 1277..1279
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1295..1300
FT /evidence="ECO:0007829|PDB:4N1A"
FT TURN 1301..1303
FT /evidence="ECO:0007829|PDB:4N1A"
FT STRAND 1304..1312
FT /evidence="ECO:0007829|PDB:4N1A"
SQ SEQUENCE 1315 AA; 145547 MW; F2C5AC3BFCCB68DE CRC64;
MSTVLVRRKE RRQPPQMPRG EILLESPPEL PEVVTNSFQN VLMYLPMAAG SAAMVFTFLN
HRNTLQLVAG GMFALSMFGM MFGQLSQQSG ERKTKLNSAR RDYLRYLGQV RQRVRKAAKQ
QREALEWNNP APGRLWSMVM SPRLWERRSS DADFAQVRIG AGPQRLAVQL IPPETKPVED
LEPMSAGALR RFLRAHSTVP DLPVAISLRS FARILPDGDP KAVYGMVRAL IMQLAAFHSP
DDVRITVCAS RERMPQWQWM KWLPHSLHPT EYDAAGQVRL LTHSLVELES MLGPEIKDRG
MFGASRAPAE PFHLVIVDGG QASYDSQIAS DGIDGVCVID LTGSVAETNE ATMLRLRVTP
ERVYVVKRDR AGKEVLSSVG RPDQASIAEA EALARQLAPF RTSAADEPEE DVLSANMTLT
SLLHIDNPYN LDPAVLWRPR PQRNRLRVPI GLDADGRPLE LDIKESAQGG MGPHGLCIGA
TGSGKSELLR TLVLALAMTH SPEVLNFVLV DFKGGATFLG MEGLRHVSAI ITNLEEELPL
VDRMYDALHG EMVRRQEHLR HSGNYASLRD YEKARMEGAP LPPMPTLFIV LDEFSELLSA
KPDFAELFVM IGRLGRSLGV HLLLASQRLE EGKLRGLDTH LSYRIGLRTF SAMESRVVLG
VPDAYELPPS PGNGYLKFAT EPLVRFKAAY VSGPVDEEPQ TRSEGPQIVR QVLPYLTDYI
RPQVVEQPQP EQRAEENKSS ESLFDVVVRQ LAGHGPEPHQ IWLPPLDVPP TLDELLPPLS
PSAAHGYTAD GWEWRGRLHA VVGLVDRPFD QRRDPYWLDL SGGAGHVGVA GGPQTGKSTM
LRTLITSLAL LHTPQEVQFY CLDFGGGTLA GLAELPHVGS VATRLDADRI RRTVAEVSAL
LEQREQEFTE RGIDSMATYR RLRATGEYAG DGFGDVFLVV DNWLTLRQDY EALEDSITQL
AARGLGYGIH VVLSSNKWSE FRTSIRDLLG TKLELRLGDP YESEVDRKKA ANVPENRPGR
GLTRDGYHFL TALPRIDGDT SAETLTEGIA TTVKTIREAW HGPTAPPVRM LPNVLPAAQL
PSAAESGTRI PIGIDEDSLS PVYLDFNTDP HFLVFGDTEC GKSNLLRLIT AGIIERYTPQ
QARLIFIDYS RSLLDVATTE HQIGYAASST AASSLVRDIK GAMEARLPPP DLTPEQLRSR
SWWTGAELFL VVDDYEMVAT SDNPLRPLAE LLPQARDIGL HLIIARSMGG AGRALYEPII
QRIKEMASPG LVMSGNKDEG ILLGNVKPHK LPQGRGYFVE RRSGTRLIQT AYRES
