ECCC5_MYCTU
ID ECCC5_MYCTU Reviewed; 1391 AA.
AC P9WNA5; L0T992; O53934; O53935; Q8VJW6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=ESX-5 secretion system protein EccC5 {ECO:0000305};
DE AltName: Full=ESX conserved component C5 {ECO:0000303|PubMed:19876390};
DE AltName: Full=Type VII secretion system protein EccC5 {ECO:0000305};
DE Short=T7SS protein EccC5 {ECO:0000305};
GN Name=eccC5 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv1783;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NOMENCLATURE.
RX PubMed=19876390; DOI=10.1371/journal.ppat.1000507;
RA Bitter W., Houben E.N., Bottai D., Brodin P., Brown E.J., Cox J.S.,
RA Derbyshire K., Fortune S.M., Gao L.Y., Liu J., Gey van Pittius N.C.,
RA Pym A.S., Rubin E.J., Sherman D.R., Cole S.T., Brosch R.;
RT "Systematic genetic nomenclature for type VII secretion systems.";
RL PLoS Pathog. 5:E1000507-E1000507(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=22340629; DOI=10.1111/j.1365-2958.2012.08001.x;
RA Bottai D., Di Luca M., Majlessi L., Frigui W., Simeone R., Sayes F.,
RA Bitter W., Brennan M.J., Leclerc C., Batoni G., Campa M., Brosch R.,
RA Esin S.;
RT "Disruption of the ESX-5 system of Mycobacterium tuberculosis causes loss
RT of PPE protein secretion, reduction of cell wall integrity and strong
RT attenuation.";
RL Mol. Microbiol. 83:1195-1209(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22925462; DOI=10.1111/j.1365-2958.2012.08206.x;
RA Houben E.N., Bestebroer J., Ummels R., Wilson L., Piersma S.R.,
RA Jimenez C.R., Ottenhoff T.H., Luirink J., Bitter W.;
RT "Composition of the type VII secretion system membrane complex.";
RL Mol. Microbiol. 86:472-484(2012).
RN [6]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=23284869; DOI=10.1371/journal.pone.0052059;
RA Di Luca M., Bottai D., Batoni G., Orgeur M., Aulicino A., Counoupas C.,
RA Campa M., Brosch R., Esin S.;
RT "The ESX-5 associated eccB-EccC locus is essential for Mycobacterium
RT tuberculosis viability.";
RL PLoS ONE 7:E52059-E52059(2012).
CC -!- FUNCTION: Part of the ESX-5 specialized secretion system, which is
CC responsible for the secretion of EsxN and a number of PE_PGRS and PPE
CC proteins, including PPE41. {ECO:0000269|PubMed:22340629,
CC ECO:0000269|PubMed:22925462, ECO:0000269|PubMed:23284869}.
CC -!- SUBUNIT: Part of the ESX-5 / type VII secretion system (T7SS), which is
CC composed of cytosolic and membrane components. The ESX-5 membrane
CC complex is composed of EccB5, EccC5, EccD5 and EccE5.
CC {ECO:0000250|UniProtKB:B2HST4}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B2HST4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutants are defective in the secretion of EsxN,
CC PPE41 and PE_PGRS proteins. {ECO:0000269|PubMed:22925462}.
CC -!- MISCELLANEOUS: Part of the eccB5-eccC5 operon, which is essential for
CC in vitro growth. {ECO:0000269|PubMed:23284869}.
CC -!- CAUTION: Was originally thought to be the product of two separate ORFs,
CC eccCa5 and eccCb5. {ECO:0000305|PubMed:19876390}.
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DR EMBL; AL123456; CCP44550.1; -; Genomic_DNA.
DR PIR; A70929; A70929.
DR PIR; B70929; B70929.
DR RefSeq; WP_003408799.1; NZ_NVQJ01000037.1.
DR RefSeq; YP_007410461.1; NC_000962.3.
DR PDB; 6J18; X-ray; 2.00 A; A=1116-1391.
DR PDB; 7NP7; EM; 4.03 A; C1/C2/C3/C4/C5/C6=1-1391.
DR PDB; 7NPR; EM; 3.82 A; C1/C2/C3/C4/C5/C6=1-1391.
DR PDB; 7NPT; EM; 3.27 A; C1=1-1391.
DR PDB; 7NPU; EM; 4.48 A; C1/C2/C3/C4/C5/C6=1-1391.
DR PDB; 7NPV; EM; 6.66 A; C1/C2/C3/C4/C5/C6=1-1391.
DR PDBsum; 6J18; -.
DR PDBsum; 7NP7; -.
DR PDBsum; 7NPR; -.
DR PDBsum; 7NPT; -.
DR PDBsum; 7NPU; -.
DR PDBsum; 7NPV; -.
DR AlphaFoldDB; P9WNA5; -.
DR SMR; P9WNA5; -.
DR STRING; 83332.Rv1783; -.
DR PaxDb; P9WNA5; -.
DR DNASU; 885898; -.
DR GeneID; 885898; -.
DR KEGG; mtu:Rv1783; -.
DR TubercuList; Rv1783; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; -; 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; 2.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 2.
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 inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1391
FT /note="ESX-5 secretion system protein EccC5"
FT /id="PRO_0000393433"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 476..678
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 858..1052
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 1161..1354
FT /note="FtsK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 499..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 876..883
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 1178..1185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT HELIX 1132..1139
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1145..1147
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1153..1157
FT /evidence="ECO:0007829|PDB:6J18"
FT TURN 1158..1160
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1163..1165
FT /evidence="ECO:0007829|PDB:6J18"
FT TURN 1168..1170
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1174..1179
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1184..1198
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1199..1201
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1215..1221
FT /evidence="ECO:0007829|PDB:6J18"
FT TURN 1233..1235
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1236..1240
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1243..1258
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1268..1272
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1281..1287
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1289..1291
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1299..1302
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1304..1306
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1310..1312
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1315..1323
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1327..1329
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1333..1340
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1345..1347
FT /evidence="ECO:0007829|PDB:6J18"
FT HELIX 1352..1354
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1356..1358
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1370..1374
FT /evidence="ECO:0007829|PDB:6J18"
FT STRAND 1379..1384
FT /evidence="ECO:0007829|PDB:6J18"
SQ SEQUENCE 1391 AA; 152740 MW; DC7B8D899AD21820 CRC64;
MKRGFARPTP EKPPVIKPEN IVLSTPLSIP PPEGKPWWLI VVGVVVVGLL GGMVAMVFAS
GSHVFGGIGS IFPLFMMVGI MMMMFRGMGG GQQQMSRPKL DAMRAQFMLM LDMLRETAQE
SADSMDANYR WFHPAPNTLA AAVGSPRMWE RKPDGKDLNF GVVRVGVGMT RPEVTWGEPQ
NMPTDIELEP VTGKALQEFG RYQSVVYNLP KMVSLLVEPW YALVGEREQV LGLMRAIICQ
LAFSHGPDHV QMIVVSSDLD QWDWVKWLPH FGDSRRHDAA GNARMVYTSV REFAAEQAEL
FAGRGSFTPR HASSSAQTPT PHTVIIADVD DPQWEYVISA EGVDGVTFFD LTGSSMWTDI
PERKLQFDKT GVIEALPRDR DTWMVIDDKA WFFALTDQVS IAEAEEFAQK LAQWRLAEAY
EEIGQRVAHI GARDILSYYG IDDPGNIDFD SLWASRTDTM GRSRLRAPFG NRSDNGELLF
LDMKSLDEGG DGPHGVMSGT TGSGKSTLVR TVIESLMLSH PPEELQFVLA DLKGGSAVKP
FAGVPHVSRI ITDLEEDQAL MERFLDALWG EIARRKAICD SAGVDDAKEY NSVRARMRAR
GQDMAPLPML VVVIDEFYEW FRIMPTAVDV LDSIGRQGRA YWIHLMMASQ TIESRAEKLM
ENMGYRLVLK ARTAGAAQAA GVPNAVNLPA QAGLGYFRKS LEDIIRFQAE FLWRDYFQPG
VSIDGEEAPA LVHSIDYIRP QLFTNSFTPL EVSVGGPDIE PVVAQPNGEV LESDDIEGGE
DEDEEGVRTP KVGTVIIDQL RKIKFEPYRL WQPPLTQPVA IDDLVNRFLG RPWHKEYGSA
CNLVFPIGII DRPYKHDQPP WTVDTSGPGA NVLILGAGGS GKTTALQTLI CSAALTHTPQ
QVQFYCLAYS STALTTVSRI PHVGEVAGPT DPYGVRRTVA ELLALVRERK RSFLECGIAS
MEMFRRRKFG GEAGPVPDDG FGDVYLVIDN YRALAEENEV LIEQVNVIIN QGPSFGVHVV
VTADRESELR PPVRSGFGSR IELRLAAVED AKLVRSRFAK DVPVKPGRGM VAVNYVRLDS
DPQAGLHTLV ARPALGSTPD NVFECDSVVA AVSRLTSAQA PPVRRLPARF GVEQVRELAS
RDTRQGVGAG GIAWAISELD LAPVYLNFAE NSHLMVTGRR ECGRTTTLAT IMSEIGRLYA
PGASSAPPPA PGRPSAQVWL VDPRRQLLTA LGSDYVERFA YNLDGVVAMM GELAAALAGR
EPPPGLSAEE LLSRSWWSGP EIFLIVDDIQ QLPPGFDSPL HKAVPFVNRA ADVGLHVIVT
RTFGGWSSAG SDPMLRALHQ ANAPLLVMDA DPDEGFIRGK MKGGPLPRGR GLLMAEDTGV
FVQVAATEVR R
