ECCC_GEOTN
ID ECCC_GEOTN Reviewed; 1479 AA.
AC A4IKE7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN Synonyms=essC {ECO:0000303|PubMed:27130157}; OrderedLocusNames=GTNG_0419;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
RN [2] {ECO:0007744|PDB:4LYA}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 921-1479 IN COMPLEX WITH 2 ATP,
RP ELECTRON MICROSCOPY, POSSIBLE FUNCTION, DOMAIN, AND PROBABLE TOPOLOGY.
RC STRAIN=W9A21 / NM16-2;
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).
RN [3] {ECO:0007744|PDB:5FV0, ECO:0007744|PDB:5FWH}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 1-196, X-RAY CRYSTALLOGRAPHY
RP (2.91 ANGSTROMS) OF 966-1479 IN COMPLEX WITH 1 ATP, POSSIBLE FUNCTION,
RP SUBUNIT, AND ATP-BINDING.
RC STRAIN=NG80-2;
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).
CC -!- FUNCTION: Part of the ESX specialized secretion system, which exports
CC proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (By
CC similarity). Might be the translocase subunit (PubMed:25865481).
CC Probably only the first FtsK domain can hydrolyze ATP
CC (PubMed:27130157). {ECO:0000250|UniProtKB:P9WNB1,
CC ECO:0000250|UniProtKB:P9WNB3, ECO:0000305|PubMed:25865481,
CC ECO:0000305|PubMed:27130157}.
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 activity
CC (By similarity). {ECO:0000250|UniProtKB:D1A4G7}.
CC -!- SUBUNIT: Whole protein oligomerizes in native gels (PubMed:27130157).
CC Part of the ESX / type VII secretion system (T7SS), which is composed
CC of cytosolic and membrane components. The ESX membrane complex is
CC composed of EccB, EccC and EccD (By similarity).
CC {ECO:0000250|UniProtKB:P9WNB1, ECO:0000250|UniProtKB:P9WNB3,
CC ECO:0000269|PubMed:27130157}.
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 480 to 599 form an unnamed domain) plus the 3 FtsK (ATPase)
CC domains which are connected by short linkers (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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000557; ABO65801.1; -; Genomic_DNA.
DR RefSeq; WP_011886773.1; NC_009328.1.
DR PDB; 4LYA; X-ray; 2.45 A; A=921-1479.
DR PDB; 5FV0; X-ray; 2.91 A; A/B=966-1479.
DR PDB; 5FWH; X-ray; 2.06 A; A=1-196.
DR PDBsum; 4LYA; -.
DR PDBsum; 5FV0; -.
DR PDBsum; 5FWH; -.
DR AlphaFoldDB; A4IKE7; -.
DR SMR; A4IKE7; -.
DR STRING; 420246.GTNG_0419; -.
DR EnsemblBacteria; ABO65801; ABO65801; GTNG_0419.
DR KEGG; gtn:GTNG_0419; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_003134_2_1_9; -.
DR OMA; WEWMKWL; -.
DR OrthoDB; 7548at2; -.
DR BRENDA; 7.4.2.8; 705.
DR Proteomes; UP000001578; 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; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR023839; Firmicutes_EssC_C.
DR InterPro; IPR022206; Firmicutes_EssC_N.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR Pfam; PF12538; FtsK_SpoIIIE_N; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 3.
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; Coiled coil; Membrane;
KW Nucleotide-binding; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1479
FT /note="ESX secretion system protein EccC"
FT /id="PRO_0000438308"
FT TOPO_DOM 1..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..259
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..1479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25865481"
FT DOMAIN 652..848
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 984..1168
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 1267..1444
FT /note="FtsK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT COILED 291..321
FT /evidence="ECO:0000255"
FT ACT_SITE 785
FT /evidence="ECO:0000305|PubMed:25865481"
FT BINDING 672..679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 1004..1009
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289,
FT ECO:0000269|PubMed:25865481, ECO:0000269|PubMed:27130157,
FT ECO:0007744|PDB:4LYA, ECO:0007744|PDB:5FV0"
FT BINDING 1036
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27130157,
FT ECO:0007744|PDB:5FV0"
FT BINDING 1105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27130157,
FT ECO:0007744|PDB:5FV0"
FT BINDING 1197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27130157,
FT ECO:0007744|PDB:4LYA, ECO:0007744|PDB:5FV0"
FT BINDING 1206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27130157,
FT ECO:0007744|PDB:4LYA, ECO:0007744|PDB:5FV0"
FT BINDING 1287..1291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289,
FT ECO:0007744|PDB:4LYA"
FT BINDING 1475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:4LYA"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 23..35
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 57..69
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:5FWH"
FT STRAND 969..978
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 979..982
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 983..990
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 991..994
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 997..1000
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1007..1021
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 1024..1026
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1027..1033
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1035..1037
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1041..1044
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1048..1053
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1057..1080
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1086..1089
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1099..1105
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1108..1113
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1115..1126
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 1129..1132
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1133..1140
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1147..1150
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1155..1158
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1164..1170
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1175..1177
FT /evidence="ECO:0007829|PDB:5FV0"
FT STRAND 1184..1197
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1199..1201
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1206..1223
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1224..1226
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1242..1248
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1257..1263
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 1264..1266
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1269..1273
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 1274..1276
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1280..1284
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1290..1300
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1301..1304
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1307..1312
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1320..1322
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1326..1331
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1334..1357
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1372..1377
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1379..1382
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1390..1398
FT /evidence="ECO:0007829|PDB:4LYA"
FT TURN 1402..1405
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1406..1413
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1414..1417
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1423..1428
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1434..1438
FT /evidence="ECO:0007829|PDB:4LYA"
FT HELIX 1440..1442
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1444..1446
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1461..1466
FT /evidence="ECO:0007829|PDB:4LYA"
FT STRAND 1469..1474
FT /evidence="ECO:0007829|PDB:4LYA"
SQ SEQUENCE 1479 AA; 168659 MW; A558E1C3898217C1 CRC64;
MSQLWVLYET YCQLFSLTNE EKVIVIGNQL EHHVTVSSFS FRNGYIQIEK KSDGSTLAVL
QGGRQIGELK PRCSITIDVD GQQMTIAWSG EEQRKYVYYV GQQSEVLVSN DPQADIETTN
ARFSLRKHRG QWVVIPDDDA PLFLNGVQLS DAVSLRNGDV LLCPYMQFVF IEEDLLAVTS
SEEVVSSLTE TMPPLSEMKK KYPMYRRTPR MIYELPSDKV SISFPSQEGD GDPRGLWLMV
LPPVMMLLVI GAVALIQPRG VFIMISIAMF ATTIVTSTAQ YMREKKARQM RKEKRRRIYT
NYLEQKREEL QALSEKQRNV LYYHFPSFEQ MKSFVMQVNS RIWERTAESA DFLHVRIGTA
DVPATYEVSV SMGDLANREI DDLLEQAQHI AKVYQTVKHV PLPIDVSHGA IGMVGKRSIV
NGEIEQLVGQ IAFFHSYHDV RFVAIFSEDD YKHWEWMKWL PHFQLPNSFA KGLIYNEQTR
DQLLSSIYEM LRERALDEEK DKKRFSPHFV FIVADRSLIA EHVILEYLEE KNEDIGISVI
FASETKESLT ENVHTLVQYI NEREGEIVIQ HRKAAHIPFQ LDEHSTEGNE SFARMLRSLN
HQKGMSNSIP EKVTFLEMMQ TRRANELQIV QNWLSCQTSR SLAVPIGLKG RNDVVELNLH
EKAHGPHGLV AGTTGSGKSE LLQTYILSLA VHFHPHEVAF LIIDYKGGGM AQPFKNMPHL
LGTITNIHGS KNFSARALAS INSELKKRQR LFDRYEVNHI NDYMELYKQG KAEQPLPHLF
LIADEFAELK SEEPDFIREL VSAARIGRSL GVHLILATQK PRGVIDEQIW SNARFRISLK
MQDVNDSKEI LRNGDAAAIT VPGRAYLQVG NNEVYELFQS AWSGAPYVEE GVEAEDEIHI
VTDLGLVPVS NVATDRKRSR QKPKTEIEMV VEQIIETQKQ LNIEKLPSPW LPPLPPRLAR
PASVTAEANA FPIGLKDEPE LQSQSDYFYQ WLEDGNIGIF GSAGYGKSTT MMTLLLSFAG
AYNPAQLHYY IFDFGNSALL PLRQLPHTAD YFRLDDEKKI EKFIKFMKEE MEQRKQRFME
KEVSTIKLYN ALSEEKLPII IVALDNFDVV KEEMPDFETQ LIQYARDGQS LGIFFIMTAT
RVSGIRPPLM NNLKTKIVHY FIDSSEKFSL IGRTPYDVDP IPGRALIKKD NAALTQIYLP
ADGEDDIEVL ENVKREMERL KEVYQHIPKP KPIPMLPPRL SMSVFTNTYV QHRASGFIPV
GLDEQTVRPV AINMRTDPHC LIVGQSRKGK TNVVKVILES LLVQEPESIG LLDGIDRGLA
GYANRDDITY IEAKERLAQW LNEADAVLQQ REREYIQAVN ENRATTLAWP PVVFVVDSLL
RLQQETDSIM QGRIANMMKQ YSHLGFHVFV AGNANEFVKG FDALTAELKQ IRQAILVTKK
SEQSLFALPF TRNEQEIEPG FGYFVVGGKD QKIQIPKVE
