ECCC3_MYCS2
ID ECCC3_MYCS2 Reviewed; 1325 AA.
AC A0QQ40;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ESX-3 secretion system protein EccC3 {ECO:0000250|UniProtKB:P9WNA9};
DE AltName: Full=ESX conserved component C3 {ECO:0000250|UniProtKB:P9WNA9};
DE AltName: Full=Type VII secretion system protein EccC3 {ECO:0000250|UniProtKB:P9WNA9};
DE Short=T7SS protein EccC3 {ECO:0000250|UniProtKB:P9WNA9};
GN Name=eccC3 {ECO:0000303|PubMed:24803520};
GN OrderedLocusNames=MSMEG_0617 {ECO:0000312|EMBL:ABK70420.1},
GN MSMEI_0601 {ECO:0000312|EMBL:AFP37082.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION.
RX PubMed=19846780; DOI=10.1073/pnas.0900589106;
RA Siegrist M.S., Unnikrishnan M., McConnell M.J., Borowsky M., Cheng T.Y.,
RA Siddiqi N., Fortune S.M., Moody D.B., Rubin E.J.;
RT "Mycobacterial Esx-3 is required for mycobactin-mediated iron
RT acquisition.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18792-18797(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24803520; DOI=10.1128/mbio.01073-14;
RA Siegrist M.S., Steigedal M., Ahmad R., Mehra A., Dragset M.S.,
RA Schuster B.M., Philips J.A., Carr S.A., Rubin E.J.;
RT "Mycobacterial Esx-3 requires multiple components for iron acquisition.";
RL MBio 5:E01073-E01073(2014).
CC -!- FUNCTION: Part of the ESX-3 specialized secretion system, which is
CC required for siderophore-mediated iron acquisition and for the
CC secretion of EsxH and EsxG. {ECO:0000269|PubMed:19846780,
CC ECO:0000269|PubMed:24803520}.
CC -!- SUBUNIT: Part of the ESX-3 / type VII secretion system (T7SS), which is
CC composed of cytosolic and membrane components. The ESX-3 membrane
CC complex is composed of EccB3, EccC3, EccD3 and EccE3.
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: Deletion of the gene impairs iron-bound
CC mycobactin utilization and EsxG and EsxH export.
CC {ECO:0000269|PubMed:24803520}.
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DR EMBL; CP000480; ABK70420.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37082.1; -; Genomic_DNA.
DR RefSeq; WP_011727068.1; NZ_SIJM01000009.1.
DR RefSeq; YP_885028.1; NC_008596.1.
DR PDB; 6LAR; EM; 3.70 A; F/J=1-431.
DR PDB; 6SGW; EM; 3.80 A; F/J=2-402.
DR PDB; 6SGX; EM; 3.70 A; F=2-402.
DR PDB; 6UMM; EM; 3.70 A; E/J=1-403.
DR PDBsum; 6LAR; -.
DR PDBsum; 6SGW; -.
DR PDBsum; 6SGX; -.
DR PDBsum; 6UMM; -.
DR AlphaFoldDB; A0QQ40; -.
DR SMR; A0QQ40; -.
DR STRING; 246196.MSMEI_0601; -.
DR PRIDE; A0QQ40; -.
DR EnsemblBacteria; ABK70420; ABK70420; MSMEG_0617.
DR EnsemblBacteria; AFP37082; AFP37082; MSMEI_0601.
DR GeneID; 66738795; -.
DR KEGG; msg:MSMEI_0601; -.
DR KEGG; msm:MSMEG_0617; -.
DR PATRIC; fig|246196.19.peg.613; -.
DR eggNOG; COG1674; Bacteria.
DR OMA; DGIYDPP; -.
DR OrthoDB; 7548at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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; -; 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; 3.
DR TIGRFAMs; TIGR03924; T7SS_EccC_a; 1.
DR TIGRFAMs; TIGR03925; T7SS_EccC_b; 1.
DR PROSITE; PS50901; FTSK; 2.
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..1325
FT /note="ESX-3 secretion system protein EccC3"
FT /id="PRO_0000434991"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 454..660
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 808..994
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 1080..1268
FT /note="FtsK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 477..484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 827..834
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 1097..1104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1325 AA; 144698 MW; 7EC038ABC91AD4F0 CRC64;
MSRLIFEHQR RLTPPTTRKG TITIEPPPQL PRVVPPSLLR RVLPFLIVIL IVGMIVALFA
TGMRLISPTM LFFPFVLLLA ATALYRGGDN KMRTEEVDAE RADYLRYLSV VRDNVRAHAA
EQRAALEWSH PEPEVLATIP GTRRQWERDP RDRDFLVLRA GRHDVPLDAA LKVKDTADEI
DLEPVAHSAL RGLLDVQRTV RDAPTGLDVA KLARITVIGE ADEARAAIRA WIAQAVTWHD
PTMLGVALAA PDLESGDWSW LKWLPHVDVP NEADGVGPAR YLTTSTAELR ERLAPALADR
PLFPAESGAA LKHLLVVLDD PDADPDDIAR KPGLTGVTVI HRTTELPNRE QYPDPERPIL
RVADGRIERW QVGGWQPCVD VADAMSAAEA AHIARRLSRW DSNPGYIRST STGSATFTTL
LGIPDASALD VASLWAPRPR DEELRVPIGV TSTGEPLYFD LKDEAEGGMG PHGLMIGMTG
SGKSQTLMSI LLSLLTTHPA DRLIVIYADF KGEAGADIFR HFPQVVAVIS NMAEKRSLAD
RFADTLRGEV ARREQILKEA GRRVQGSAFN SVAEYESAIA AGHDLPPMPT LFVVADEFTL
MLAEHPEYAD LFDYVARKGR SFRIHLLFAS QTLDVGRIKD IDKNTSYRIG LKVASPSISR
QIIGVEDAYH IESGREHKGE GFLVPAPGAV PIKFRSTYVD GIYDPPRAEK SIVVHALPQP
QVFTAGRVEP EPDTVIATGD VEVHTAPPRK LIATIGDQLA AYGPKAPQLW LPPLDEPIAL
ADVLAGADVE PGQLRWPLGE IDKPFEMRRD VLVYDAHTAA ANVLIHGGPR SGKSTALQAF
VLSAAALHSP RAITFYCLDY GGGKLADLAD LAHVGSVATP LEPERIRRTF GELEQLLRAR
QRQGAVNRTG SYTDGYGEVF LVIDNLYAFS RDNTDTFNTR NPLLAKVTEL ANSGLAYGIH
VVITTPNWLE VPLAMRDGLG LRLELKLHDS HDSIVRVAGA LRRPADSVPA DQPGRGLTMA
AEHFLFAEPA LSDIAVINAR YPGVSAPPVR LLPTDLSPDA LAPLYPAPET VVIGQREEDL
APVAVDFANH PLLMVFGDSK SGKTTLLRHI IRTVRENSTP DQVAFTVIDR RLHLVDEPLF
PDNEYTANID RVLPAMLGLS ALIEKRRPPA GLSAQELSRW TYTGHTHYLI VDDVDQIPDT
PAVSGPFVGQ RPWTNIVGLL AEAADLGLRV IVTARATGSA HAVMTAPLLR RLNDLQATTL
MLSGNPTDSG KIRGHRFARF PAGRGLLLTD TDTPDHIQLV NPLGDAALSG NIGNNGNHNR
GGEYR
