ID B4SED3_PELPB Unreviewed; 825 AA.
AC B4SED3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Cell divisionFtsK/SpoIIIE {ECO:0000313|EMBL:ACF44552.1};
DE Flags: Precursor;
GN OrderedLocusNames=Ppha_2359 {ECO:0000313|EMBL:ACF44552.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44552.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF44552.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001110; ACF44552.1; -; Genomic_DNA.
DR RefSeq; WP_012509026.1; NC_011060.1.
DR AlphaFoldDB; B4SED3; -.
DR STRING; 324925.Ppha_2359; -.
DR KEGG; pph:Ppha_2359; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_9_10; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000002724; Chromosome.
DR GO; GO:0005886; C:plasma 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; 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; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 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:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:ACF44552.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000002724};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..671
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 218..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 825 AA; 91763 MW; DEED85C32309333E CRC64;
MKNNNKGVKG TPLDMKALQK EIGGLVLMLL ALFLIAALLS FHPDDEASFG TLAWHDIFSR
SARDVAESIH NPFGLFGARI SAFFIRSFLG YSVILPLTAI FLWGWLLLRA KSLKPAILFS
LYSLAFSLDI ATMFGLTSAP FSDMMAGAIG RMLAEFLSVV IGFTAALVLL SVIALVLTLY
MGQTALAEGM RLVLAAVKSS VRSFAAFRAK RAEKRKKKAE LQKLKEKKRE EKREEKRKLA
LKKEAQKKEE LKKQTLKQEP ESEPFVSASA VPLVTPVFQE ELLLPEPPLP EPSAAERTPL
ALQSKIPGEP EMIIHQAVRE KEADLDERRL KVQTKDREPY RFPSIDLLEK VPDDNDQIDQ
QHLDESKRKL LEKLKIYKIE VKRISTTVGP RVTLFELELE PDVKVSRVKS LENDLAMALS
ARGIRIIAPI PGKNAVGVEI PNGKPKTVWL RSVLQVEKFK NSTMMLPIVL GKTIANEVYI
ADLATMPHLL IAGATGAGKS VCINVIISSL LYACSPDKVK FVLIDPKRVE LFQYQHLKNH
FLMRFPGIEE QIITDPQKAV YALKCVVKEM EIRYETLEKA GVRNIGDHNR RIPEEALPYI
VVVIDELADL MITAGREVEE PIIRIAQLAR AVGIHLIVAT QRPSVDVITG IIKANFPARI
AFQVASRVDS RTILDGSGAE QLLGNGDMLY QPSNQPKSMR IQGPYVSSGE VEEITSFIGS
QHALKNMYVL PSPDINKGNG ISSSGYQEKD GKDSMFEEAA RLVVTHQQAS VSLLQRRLRL
GFSRAGRVMD QLEFSGIVSE ADGSKAREVL IQNEDSLELL LRNLD
//
