ID A0A2J9DX76_9GAMM Unreviewed; 1057 AA.
AC A0A2J9DX76;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=A6J60_004130 {ECO:0000313|EMBL:PNK60137.1};
OS Psychrobacter sp. FDAARGOS_221.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK60137.1, ECO:0000313|Proteomes:UP000217719};
RN [1] {ECO:0000313|Proteomes:UP000217719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719};
RA Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA Aluvathingal J., Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2017) 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}.
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:PNK60137.1}.
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; NWFK02000001; PNK60137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J9DX76; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000217719; Unassembled WGS sequence.
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};
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};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 706..920
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 193..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 723..730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1057 AA; 115788 MW; 3F21866821E18DD7 CRC64;
MITAHFLHSS KKVIFTLLAV LVSAFLFVIL LTYTPNDPSW SRISSDMGQV SNMGGAIGAW
MSDLLYTFFG WSAWWLIVFL AYEALCIWWQ RNQAIGPLRV IGYVFLLLSS CALVAIIPQL
LSISEVSSAR VGGILGAEIA TRLTGLLTIY GTAAFLLLFV LLTATFSFDI HWRQVLKSLF
SLSWLGNGVR DKQAHADEQS EEDAQVDTEH DSDSEDSDED GYQLGDPEAE QPMYQQLKLN
LDEQQAQQEA EQAQDPAWNN ALDEFLVSSG LTESIMNLRE QKKQEAQAQR ELKAKQEAAA
ESQPTVKQEP SFAWNDPDVI DELLDDGNGS QSQPTQAENP VDGQPSTSQP STTQSQTAPV
EAQQIQAEQT EFEQDNSELS AAIESTEIEI APEVDPVPDT APTTESIDDS ITADLTAESE
SMLADENTAE TSPAFSEDNS SEDNSDSAEE EQAHEVSAQQ EVSAQQASEQ DVSTDQEQPA
EPEAFVDLTP TNTPPSNPRE PHKAEDKSKA SQPVTPTIRF ATPEGDGNHI EDMVPDSDDE
VALPEIHDDA AFASSSRAMQ TAKYRESLTP IPEISILDKP DPDRKPSYTQ EELKQLSELL
EIKLQEFNVK AEVVNAIPGP VVTRFEVDLA AGVKASKVTG ISRDLARSLS MASLRVVEVI
PGKPYIGIEV PNKKREMVRL IELLKTEAYQ DPKAQISMAM GKDIGGKPII TDLARAPHML
VAGTTGSGKS VLVNAMLLSM LLKYKPSELR LILIDPKQLE LANYNDIPHL LTPVVTDMNE
AASSLSWCVA EMERRYQLMS LLKVRKLGEF NKKVIAAEKA GRPILDPLWR PNDSVSIDKA
PKLKTLPMIV IVADEFADMI MQVGKQAEEL ITRLAQKSRA AGIHLMLATQ RPSVDVITGL
IKANIPVRAA LRVNSKVDSR TILDAGGAED MLGNGDMLFL GPGQIEPDRV HGAYVSDEEV
NRVCDAWRER GAPDYIDNMA SNFELTSPSS GGNTSGEDDA LYDEAVAFVL ETRKVSASSI
QRKFSIGYNR AARIVDSMEE AGLVSPMGKS GKRELLM
//
