ID A0A145X0H1_9GAMM Unreviewed; 1051 AA.
AC A0A145X0H1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=AMD27_03570 {ECO:0000313|EMBL:AMW78059.1};
OS Acinetobacter sp. TGL-Y2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW78059.1, ECO:0000313|Proteomes:UP000076238};
RN [1] {ECO:0000313|Proteomes:UP000076238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA Zhang G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015110; AMW78059.1; -; Genomic_DNA.
DR RefSeq; WP_067656441.1; NZ_CP015110.1.
DR AlphaFoldDB; A0A145X0H1; -.
DR STRING; 1407071.AMD27_03570; -.
DR KEGG; acv:AMD27_03570; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000076238; 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:AMW78059.1};
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:UP000076238};
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 67..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 697..911
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 198..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 714..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1051 AA; 116765 MW; E6529068FB05DA46 CRC64;
MTAVSSVYAQ RLVLTFFLIS FGIYLFLATV TYTPFDPGWM HISSDTQHVS NASGVAGAWI
ADLMFGFLGW ASLLIPIFLF VEAIQVWWPR SFVSRPFRYA AQFFILLSIA SLNYLLWTVP
ADTLTNASGG IIGYELGASL SHLLTIYGAV FFLLLLTGVL FTLAFGIQWN KTWATLQATP
AYLQDLFYKN VPESESAYDL TSPSAQTPKV QNAQSQATQN NAKQNDDELN HILELDETAQ
AATTKDKRAE IMAERLFQDM VGKEAAQQFD AEDELEFERT LEKAHRLEQE NLRVVPTGEV
WKALHPDDNH KREIDELLRA AEDDLQPATQ SHLMDQARPQ RSFAQESVQS SKSDLDWNDD
QVFDELLAVV PDNQRENGMH SPFNTAPDTD EVNSTGVDLM PTAAIASGAV AAHIDPTHRA
LRRAENLASE LDDLASLVDQ SDQNYMSQHS DTALKQQQQE TQPQQATPPR TTSSYAQSTP
LVRAEIQTQF KPTSIVSEEE KQRIAADKTA FRDAWQETVG VPEVDEKPID DFDMDAPLTD
AFGRPMSLAM QVAQRRKDLP TLPGLEILDK VDPNKKVNFT PEQLARLSEL LEIKLQEFNV
KAKVIEAQPG PVVTRFELDL APGVKASKVT NISRDLARSM SMASVRVVEV IPGKPYIGIE
VPNSTREMVR LIELLETPVY RDPNSSISMA MGKDISGNPV LTDLGKAPHM LVAGTTGSGK
SVAVNAMILS MLLKYTPKQL RLILIDPKQL ELANYNDIPH LLTPVVTDMK DAVNALNWCV
NEMERRYKLM SFLKIRKLSD YNRKVEEAIA NGEDLIDPTW KASDSVVGER APRLEPLPSI
VIVADEFADM IMQVGKKAEE MITRLAQKSR AAGIHLLLAT QRPSVDVITG LIKANIPTRV
ALRVNSKIDS RTILDAGGAE DLLGHGDMLF LGPGKIEPER VHGAFISDDE VNRICDAWRE
RAAPNYVDEI LTPYDEEPTS RGFEDGDGSS DRDALYDQCV SFVLETRKAS TSSLQRKFSL
GYNRAARIID QMEENGIVSS MGANGKREIL V
//
