ID A0A1M5UZ83_9BACI Unreviewed; 858 AA.
AC A0A1M5UZ83;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SHH68194.1};
GN ORFNames=SAMN05421807_11120 {ECO:0000313|EMBL:SHH68194.1};
OS Virgibacillus chiguensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=411959 {ECO:0000313|EMBL:SHH68194.1, ECO:0000313|Proteomes:UP000184079};
RN [1] {ECO:0000313|EMBL:SHH68194.1, ECO:0000313|Proteomes:UP000184079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6496 {ECO:0000313|EMBL:SHH68194.1,
RC ECO:0000313|Proteomes:UP000184079};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXD01000011; SHH68194.1; -; Genomic_DNA.
DR RefSeq; WP_073009965.1; NZ_FQXD01000011.1.
DR AlphaFoldDB; A0A1M5UZ83; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000184079; 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 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}.
FT DOMAIN 526..718
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 49..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 543..550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 858 AA; 98310 MW; 5254B5167825432B CRC64;
MWDNWKKKIK RLFISDEENH RDEYMQQPDR HHPEAKMMYQ YPAKKSFRFP VVPDKGNETN
QHRSYSDKNE VFENRGNPKT QKPSIQEHTY SKSTEDDVSK YDTPAFRRRN HNHSKPRHTT
MQGYKDEHSK HKVYKKNPDQ PFRPTEVPSP IYGFRPRNEN KAKVIEEVPA YKRKQETDPF
KDLEVLKEGP SRTEINAVDV EVPAYQRKQA IEDVKQLANS EIQNEGYFKR NKKETNVEQK
ETINDLKEEE TYQSASMEKH EKHTDASTAN EQNHIPSESF NQKDTEEQVE TKQESAATVV
KEERSDDDQQ KEDEQTNQTK TEPKRESRLS QRRRQQQMGQ NNVPFNVMMT PRDKKNLWDR
TKQKHNKNAE ETRPSQWTNE ATDMITEHNA VQEIPLHLLN DIEDHSSDDK AWLDEQQQLL
EQTLKYFNVQ AKVVNVTQGP SVTRFEVQPQ LGVKVSKVRN LSDDLKLNMA AKDIRIEAPI
PGKNTIGIEI PNRKPQMVGL QGVFATEAFK KSNSPLTIAL GLSIEGEPLI TNIQKMPHGL
IAGATGSGKS VCINTILISL LYKAHHEEVK FLLIDPKMVE LAPYNGIPHL VSPVITDVKA
ATAALKWAVA EMEERYEKFV HEGVRDIERY NEKMVKQQQM KNKLPFIVIV IDELADLMMV
SPQDVEDAIS RIAQKARACG IHLILATQRP SVDVITGLIK ANIPTRIAFS VSSQVDSRTI
LDTSGAEKLL GKGDMLFIEN GSGKTVRLQG PFVSDDEIDR VASYTRSIAP ANYLFEQEQL
LEQIHTEEEE DELLKDAILF VLEQNGASTS LLQRHFKIGY NRAARLIDTL EQRGIISGQN
GSKPREVLVT STQVEDMI
//
