ID Q6FDR9_ACIAD Unreviewed; 1018 AA.
AC Q6FDR9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN OrderedLocusNames=ACIAD0891 {ECO:0000313|EMBL:CAG67789.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG67789.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG67789.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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}.
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DR EMBL; CR543861; CAG67789.1; -; Genomic_DNA.
DR RefSeq; WP_004922102.1; NC_005966.1.
DR AlphaFoldDB; Q6FDR9; -.
DR STRING; 202950.GCA_001485005_02639; -.
DR GeneID; 45233351; -.
DR KEGG; aci:ACIAD0891; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_7_0_6; -.
DR OrthoDB; 9807790at2; -.
DR BioCyc; ASP62977:ACIAD_RS04115-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 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; 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; 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:CAG67789.1};
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:UP000000430};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 663..877
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 196..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 680..687
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1018 AA; 113479 MW; 0F4B1DEBB95111B9 CRC64;
MTAVSSVYAQ RLLITLFLVS FGIYLFVATV TYTPFDPGWM HISSDTQNVS NASGVAGAWI
ADLMFGFLGW ASLLIPIFLF IEAIQIWWPR SFLTRPFRYA AQFFIILATS TLLYLYWNVP
ADTLENASGG IIGFEVGQSL SGLLTIYGAT LFLVAFWVLL ITLAFGIQWN RTWATLKATP
AYLQDLFYKN VSPNESDYDL TEQPKKTAST SKTTVASEQN HQDQVHDQHL EQTTRTDQKA
FDTTTKNFVS DEMVEKLFAD VVAKEQYAQQ QVQAVNTSIE DPAFEQTIQK AHQLEKEAKR
LVPTGEVWKA LQTDDSTHKQ EIDALLRAAD DNEPSVTPMT SDELLANLKA QQAQQNHTQP
NNHTAKLNWN DDQIFDELLA AMPNSKIGSD IHTPFVEHRE DTTPDHTDHL IQQVEQTLQA
SSNTLQPKNM TNLDEAEEQS DLLTETVEEN PSTHYAGQPQ NRSFTSNELT AKDQEKLSKE
EFIEAWQETA GKPVEDDFDF DAPLTDASGR PMSRAMQVAQ KRRDLPTLPG LELLDKVDPN
KKVNFTVEQL ERLSELLEIK LQEFNVKAKV VEAQPGPVVT RFELDLAPGV KASKVTNISR
DLARSMSMAS VRVVEVIPGK PYIGIEVPNS SREMVRLIEL LETASFRDPA GLLSMAMGKD
ISGNPVITDL GKAPHMLVAG TTGSGKSVAV NSMILSMLLK YTPDQLRLIL IDPKQLELAN
YNDIPHLLTP VVTDMKDAVS ALNWCVNEME RRYKLMSFLK IRKLADYNRK VEEAIANGED
LIDPTWKPSD SATQERAPRL QPLPSIVIVA DEFADMIMQV GKKAEEMITR LAQKSRAAGI
HLLLATQRPS VDVITGLIKA NIPTRVALRV NSKIDSRTIL DAGGAEDLLG HGDMLFLGPG
KIEPERVHGA FIGDDEVNRI CDAWRERGEP NYVDEILTPF DEEPTSRGFE DGGEGASDRD
MLYDQCVAFV LETRKASTSS LQRKFSLGYN RAARIIDQME ENGIVSAMGA NGKREILV
//
