ID A0A0M2SV50_9BACI Unreviewed; 893 AA.
AC A0A0M2SV50;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=WQ57_09400 {ECO:0000313|EMBL:KKK38444.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK38444.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK38444.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK38444.1,
RC ECO:0000313|Proteomes:UP000034166};
RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKK38444.1}.
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DR EMBL; LAYY01000008; KKK38444.1; -; Genomic_DNA.
DR RefSeq; WP_046523552.1; NZ_LAYY01000008.1.
DR AlphaFoldDB; A0A0M2SV50; -.
DR PATRIC; fig|1408103.3.peg.2109; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000034166; Unassembled WGS sequence.
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 GO; GO:0007059; P:chromosome segregation; 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:SF42; DNA TRANSLOCASE SFTA; 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}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000034166}.
FT DOMAIN 555..747
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 14..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 572..579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 893 AA; 100167 MW; B3883676FB67074E CRC64;
MSWIKKLFQM FSGDEENGLE SRSREVSKPL QPRDPKHFEM KKELDAKVLY QYPKGQFKFP
LIPDSPPRER ESAKPRQRPA AQDQGLADEL EPVKPKTRDK IEKHAQIKPS RHPFRPTETP
SPVFAFNRPK QSKEAEFEVK GSVSEPQPKE PAVRAPSSWS AKREADERKW EAVSKIRQEK
LAVDKIFPAP EEPASVIEYE LEDGLGLAMK PEPEEKPDFV LEQEPEEKPD FVLEQEPEEK
PEFILEQEPE EKPEFILKPE PEEKPDFVLE QEPEEKPEFI LEQEPEEKSD FIPEQGSVEV
PEFETLPQLA AADKESEQES EQETFESPDL GKTGVIAANQ TADSPSREEE PQAVGENSPQ
SPKRHLPFNV LMLKQDKRKL ENRKKEELAP VTAAVEPAIT QDKDIIGESA PNSVKETPRA
YEFPPLDLLK PPVIAATNQD WLQHQEYLLN ETLKNFNVGA KVVNVTQGPS VTRFEVQPEP
GVKVNKITNL SDDIKLSLAA KDIRIEAPIP GKHTIGIEVP NASSRPVLIS EILQTSGFQS
TASPLAVALG LDIAGSPIVT DLKKMPHGLI AGATGSGKSV CINTMLVSLL YKAHPDDVKL
LLIDPKMVEL APYNHIPHLV SPVITDVKAA TASLKWAVDE MERRYELFAH TGVRDIGRFN
ELALEHKRYH DKLPYIVIII DELADLMMMS PADVEEAICR IAQKARACGI HLIIATQRPS
VDVITGLIKA NVPTRVAFSV SSQVDSRTII DISGAEKLLG KGDMLFLENG SSKPYRLQGT
FVSDREIDEV VAFVRKQRTP EYLFEQDELL RKSQLTEEED ELFIEACSFV IEHGGASTSS
IQRRFKVGYN RAARLIDMME QHGFISEARG SKPRDVLITA SDLESFQETS TLA
//
