ID U3GVD1_9CORY Unreviewed; 962 AA.
AC U3GVD1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=CARG_05785 {ECO:0000313|EMBL:AGU15284.1};
OS Corynebacterium argentoratense DSM 44202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15284.1, ECO:0000313|Proteomes:UP000016943};
RN [1] {ECO:0000313|EMBL:AGU15284.1, ECO:0000313|Proteomes:UP000016943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15284.1};
RX PubMed=24092787;
RA Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA Ruckert C., Tauch A.;
RT "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL Genome Announc. 1:e00793-13(2013).
CC -!- FUNCTION: Essential cell division protein that coordinates cell
CC division and chromosome segregation. The N-terminus is involved in
CC assembly of the cell-division machinery. The C-terminus functions as a
CC DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC recombination site, which is located within the replication terminus
CC region. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
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; CP006365; AGU15284.1; -; Genomic_DNA.
DR RefSeq; WP_020976439.1; NC_022198.1.
DR AlphaFoldDB; U3GVD1; -.
DR STRING; 1348662.CARG_05785; -.
DR GeneID; 78249932; -.
DR KEGG; caz:CARG_05785; -.
DR PATRIC; fig|1348662.3.peg.1131; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_2_1_11; -.
DR Proteomes; UP000016943; 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: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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016943};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 574..787
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 45..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 962 AA; 101941 MW; B5725B032BC71A85 CRC64;
MPVAQRASET AEERTGSAFR GVGAGLGAAF RGTAHGLGVL TRSLGGRGRG HRYDHDDDAL
ESDSESTVDD DATVVLDSPS SSRRGHRTRA SKKSDVPALK QPQPGVVAND GGHDGIGLAL
IGIAVILGAC VWVDVAGPVG RVIADGAYYS IGAGAVVLPI ILAAAAVALM LGYLPGAQAK
QRGALGFVLL ALPMLGLIHI FAGLPSEWAG RKTAGGFLGT IVGGPLAAGL TSYIAIPILI
LVIVYGALKL TDVTVREFVT YISDIVRGAD GRYEQQQWDD VADEDDDELH IDDYRADIPS
STRPPSSARA TRSNTGARGL TPAENYPLDS HSDEPTVTLP SPRKKSRRED NLYDEASEPM
LTFDQEPSTS ARTLRPDTSA ARDAVEAAAS RLDTVAAAAG SAAAKATESA AAQAAAPAAA
VVAASRAAKA VAGTDDSVAH STDLSAAPSD DPYEVPSPHL LTPGAPAITR SEANDRTIEQ
INGVFQEFNI DAIVTGFSRG PTVTRYEVEL GRGVKVSKIT NLQANLAYAV ANENVRILSP
IPGKQAVGIE VPNTDREMVR LGDVLNAPAV ANDDNPVLIG IGKDVEGEYI AHSLAAMPHL
LVAGATGSGK SAFVNAMLVS LLTRATPEEV RLILVDPKMV ELTPYEGIPH LITPIITQPK
KAAAALNWLV EEMEQRYMDM RQAGVRHVKD YNAKIRAGKV ELPPDSKREL KPYPLIICVV
DELADLMMTA PKEIEDSIVR ITQKARAAGI HLVLATQRPS VNVVTGLIKT NVPSRLSFAT
SSQTDSRVIL DQPGAEKLIG MGDGLFIPQG GNALRIQGAY VSDEEIHAVV EKAKEQGAPH
YEENVTEEKV EKKHIDSDIG DDLDDLIEAA TLVITSQLGS TSMLQRKLRI GFAKAGRLMD
LLESRDVVGP SEGSKPREVL VREDELETTL WMLRGANPED APRDNDDQDT HIVDANPTGG
VF
//
