ECCC3_MYCTO
ID ECCC3_MYCTO Reviewed; 1330 AA.
AC P9WNA8; L0T4X3; O53689; Q7DA37;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
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:0000250|UniProtKB:P9WNA9}; OrderedLocusNames=MT0297;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Part of the ESX-3 specialized secretion system, which is
CC important for iron and zinc uptake or homeostasis.
CC {ECO:0000250|UniProtKB:P9WNA9}.
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}.
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DR EMBL; AE000516; AAK44521.1; -; Genomic_DNA.
DR PIR; B70836; B70836.
DR RefSeq; WP_003401478.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNA8; -.
DR SMR; P9WNA8; -.
DR PRIDE; P9WNA8; -.
DR EnsemblBacteria; AAK44521; AAK44521; MT0297.
DR KEGG; mtc:MT0297; -.
DR PATRIC; fig|83331.31.peg.320; -.
DR HOGENOM; CLU_003134_1_0_11; -.
DR Proteomes; UP000001020; 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; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1330
FT /note="ESX-3 secretion system protein EccC3"
FT /id="PRO_0000427159"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 456..662
FT /note="FtsK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 811..1000
FT /note="FtsK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT DOMAIN 1090..1280
FT /note="FtsK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 479..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 829..836
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 1107..1114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1330 AA; 145229 MW; 1108A7885246A853 CRC64;
MSRLIFEARR RLAPPSSHQG TIIIEAPPEL PRVIPPSLLR RALPYLIGIL IVGMIVALVA
TGMRVISPQT LFFPFVLLLA ATALYRGNDK KMRTEEVDAE RADYLRYLSV VRDNIRAQAA
EQRASALWSH PDPTALASVP GSRRQWERDP HDPDFLVLRA GRHTVPLATT LRVNDTADEI
DLEPVSHSAL RSLLDTQRSI GDVPTGIDLT KVSRITVLGE RAQVRAVLRA WIAQAVTWHD
PTVLGVALAA RDLEGRDWNW LKWLPHVDIP GRLDALGPAR NLSTDPDELI ALLGPVLADR
PAFTGQPTDA LRHLLIVVDD PDYDLGASPL AVGRAGVTVV HCSASAPHRE QYSDPEKPIL
RVAHGAIERW QTGGWQPYID AADQFSADEA AHLARRLSRW DSNPTHAGLR SAATRGASFT
TLLGIEDASR LDVPALWAPR RRDEELRVPI GVTGTGEPLM FDLKDEAEGG MGPHGLMIGM
TGSGKSQTLM SILLSLLTTH SAERLIVIYA DFKGEAGADS FRDFPQVVAV ISNMAEKKSL
ADRFADTLRG EVARREMLLR EAGRKVQGSA FNSVLEYENA IAAGHSLPPI PTLFVVADEF
TLMLADHPEY AELFDYVARK GRSFRIHILF ASQTLDVGKI KDIDKNTAYR IGLKVASPSV
SRQIIGVEDA YHIESGKEHK GVGFLVPAPG ATPIRFRSTY VDGIYEPPQT AKAVVVQSVP
EPKLFTAAAV EPDPGTVIAD TDEQEPADPP RKLIATIGEQ LARYGPRAPQ LWLPPLDETI
PLSAALARAG VGPRQWRWPL GEIDRPFEMR RDPLVFDARS SAGNMVIHGG PKSGKSTALQ
TFILSAASLH SPHEVSFYCL DYGGGQLRAL QDLAHVGSVA SALEPERIRR TFGELEQLLL
SRQQREVFRD RGANGSTPDD GFGEVFLVID NLYGFGRDNT DQFNTRNPLL ARVTELVNVG
LAYGIHVIIT TPSWLEVPLA MRDGLGLRLE LRLHDARDSN VRVVGALRRP ADAVPHDQPG
RGLTMAAEHF LFAAPELDAQ TNPVAAINAR YPGMAAPPVR LLPTNLAPHA VGELYRGPDQ
LVIGQREEDL APVILDLAAN PLLMVFGDAR SGKTTLLRHI IRTVREHSTA DRVAFTVLDR
RLHLVDEPLF PDNEYTANID RIIPAMLGLA NLIEARRPPA GMSAAELSRW TFAGHTHYLI
IDDVDQVPDS PAMTGPYIGQ RPWTPLIGLL AQAGDLGLRV IVTGRATGSA HLLMTSPLLR
RFNDLQATTL MLAGNPADSG KIRGERFARL PAGRAILLTD SDSPTYVQLI NPLVDAAAVS
GETQQKGSQS
