ID D4MMC2_9FIRM Unreviewed; 972 AA.
AC D4MMC2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE and related proteins {ECO:0000313|EMBL:CBL34905.1};
GN ORFNames=ES1_20290 {ECO:0000313|EMBL:CBL34905.1};
OS [Eubacterium] siraeum V10Sc8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=717961 {ECO:0000313|EMBL:CBL34905.1, ECO:0000313|Proteomes:UP000007050};
RN [1] {ECO:0000313|EMBL:CBL34905.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL34905.1,
RC ECO:0000313|Proteomes:UP000007050};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum V10Sc8a.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL34905.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL34905.1,
RC ECO:0000313|Proteomes:UP000007050};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FP929059; CBL34905.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MMC2; -.
DR KEGG; esr:ES1_20290; -.
DR PATRIC; fig|717961.3.peg.2158; -.
DR HOGENOM; CLU_001981_9_2_9; -.
DR BioCyc; ESIR717961:G136L-1686-MONOMER; -.
DR Proteomes; UP000007050; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 617..809
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 635..642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 972 AA; 106449 MW; CADE50F65792E92F CRC64;
MAAKHNLNNS TNEAEARTSG SSGKTRKKDQ TIEDKQRELS ERCKNDIEKE LKSKRRRSSI
ILFAIGVLMA LFTIIGFIGS LNRAEGNSLN LLDMIYSFLC GMFGFTVFFT GPILIYVAVL
IATDKSRTSI LTKILQLSGG IVILSTAIQI FFVGSVGEGT TDFFGAVASL YSDGTRLTGG
GIIGGVPAWL LLLFGNVGAI VMIILIAFVF VMLISRKSLM DFLGAVGKPV KKVAVTAKEK
HAQHKEEMEA YRLEQEQQRL QAESERKEKL IELESNAVGT PATTLQERHD ENIEEQKKDS
DNFINEINNY NGKVSPKPEE AVQQSNEHLP EIAPESDVHM SCDKLPDLPV ADNNGSAQKA
QSVAIDKQED SEPIPEYFPP LPIYPPEEVN PVEAALNSFI EETNYEQNSS VQREEQFVND
VNAPVAPPAE APFIADNTDS GIADSTPDGI TDSTAVQEDK QDGDTSDSDK LYTVTLNEED
HPLPPTALLD EIMPGKAQED IDRELETNAN TIVEALRSFG VQTKCIGTCR GPSVTRYELQ
PAAGVKISKI TGLADDIALN LASSGIRIEA PIPNKPAVGI EVPNKIRDTV PFRQLIESSD
IAEKKSKLAA VLGKDISGGI VIADIAEMPH LLIAGTTGSG KSVCVNSIIM SILFRSKPED
VKFIMIDPKA VEFMAYNGIP HLLIPVVTDP KKAAGALNWA VGEMLKRYSM FSEYNVRNIH
GYNALAAKDP EMDKMSQTVI FIDELADLIM ASKNEVEDSI CRLAQMARAA GMHLVIATQR
PTVDVVTGLI KANIPSRIAL KVSSGTDSRV IMDEQGAEKL LGKGDMLFKS VSMPKPIRVQ
GCWISDKEVE RVVDFLKNKF ELDYDDDVMK EVERQAELVK GNDKSSDSVG FESGDIDVSD
DKLEDAIRIV VENGQASVST LQRKLKLGFG RAARLVDVME EMGIVGPSQG SKPREVLMTK
EQYYERQMNK QQ
//
