ID A0A0M2T416_9BACI Unreviewed; 798 AA.
AC A0A0M2T416;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KKK39545.1};
GN ORFNames=WQ57_02320 {ECO:0000313|EMBL:KKK39545.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK39545.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK39545.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK39545.1,
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:KKK39545.1}.
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DR EMBL; LAYY01000002; KKK39545.1; -; Genomic_DNA.
DR RefSeq; WP_046522117.1; NZ_LAYY01000002.1.
DR AlphaFoldDB; A0A0M2T416; -.
DR PATRIC; fig|1408103.3.peg.532; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000034166; Unassembled WGS sequence.
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 GO; GO:0051301; P:cell division; 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: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}; Cell cycle {ECO:0000313|EMBL:KKK39545.1};
KW Cell division {ECO:0000313|EMBL:KKK39545.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 463..659
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 216..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 798 AA; 87955 MW; 6D1497F103024240 CRC64;
MAKKKRRQKS RKNDNIKTTL KYELSGLILL ALAIIAMAEM GAVGKAAVLF FRFFMGEWYM
LSLIGLVVFS VYVMWKRQLP FLLQIKLFGT YLIIGAILLL SHVTLFELLS NGGKFENASV
IANTWELFRM EAKGETSTVD LGGGMIGAVL FAMFYFLFDA AGSQLIAFVA ILIGIILITG
RTFGDAAGKM ITGTGSFIAR QWKAFIEDMK MWQENQSRKK AERTEAKKIE QQEKAAVPTA
PASPAQRETD QEKYEPSEPI ISSFAERAYP EQEDKEAASA AVPHDKSQAE NREKSKTKKQ
DGKSVDDVEE EENVPPIAFT EVENAAYELP PVNLLKLSNK TDQSGEYELI HANAAKLERT
FQSFGVKARV TQVHLGPAVT KYEVHPDVGV KVSRIVSLQD DLALALAAKD IRIEAPIPGK
SAIGIEVPNS EVAMVSLREV LEARHQNKPG AKLQIGLGRD ITGEAVLAEL NRMPHLLVAG
ATGSGKSVCI NGIITSILMK AKPHEVKLMM IDPKMVELNV YNGIPHLLAP VVTEPKKASQ
ALKKVVSEME RRYELFSHTG TRNIEGYNEY VKRHNAEEEA NQPLLPYIVV IVDELADLMM
VASSDVEDSI TRLAQMARAA GIHLIIATQR PSVDVITGVI KANIPSRIAF AVSSATDSRT
ILDMGGAEKL LGRGDMLFLP VGASKPVRVQ GAFLSDEEVE EIVEFVIGQQ KAQYQDEMIP
EDIPETTGEV DDDLYDDAVE LIIEMQTASV SMLQRRFRIG YSRAARLIDE MEQRGIVGPY
EGSKPRTVLV SKNEEASS
//
