ID A0A126PBQ4_9BACT Unreviewed; 966 AA.
AC A0A126PBQ4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AMJ65491.1};
GN ORFNames=AXW84_08655 {ECO:0000313|EMBL:AMJ65491.1};
OS Hymenobacter sp. PAMC 26628.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ65491.1, ECO:0000313|Proteomes:UP000059956};
RN [1] {ECO:0000313|EMBL:AMJ65491.1, ECO:0000313|Proteomes:UP000059956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ65491.1,
RC ECO:0000313|Proteomes:UP000059956};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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; CP014304; AMJ65491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A126PBQ4; -.
DR STRING; 1484118.AXW84_08655; -.
DR KEGG; hyz:AXW84_08655; -.
DR Proteomes; UP000059956; 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 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:AMJ65491.1};
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:UP000059956};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 608..813
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 626..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 966 AA; 102996 MW; 0E672922F79BE1AA CRC64;
MADNRYKNPP PGPSANRPAE GRPAAAPRAN APRPAAEPAP AAAPRPPRPA ATNQPKAAKA
AAQAQAARAP RGPRGPLPGV AGLKALLRDR RFHLFIGFGL LLGSLYLTIA FTSFLFTGHA
DQSVVAAMST IPTKEAGQES NNWLGLLGAW AAQVFIYKLF GVAAFALIPI VFFLGYKIVF
RTATGSVSYV LALGLFTMAW LSTLLGYVVV ALGAPAPGAD LALAHRLDFL CGGVGFEAAS
WLSSLIGWGT VLLLAFVLIS FVVFFFNITT LPFNFGRSAA QAEADEDAEL TAEIEAEEAA
KARPAAPKPA PNAPAPMALA FTAEETEDVE ETSGAPAPVE YEPAPQASSG PALSVAGPLA
TTVAAAAAVP LVVSGPSFSV EMPEPEPEVA FVAPVVATVP TPLSLADLAD GPPAKPVMGP
LGVENKQLEI TVPSRDDLDP NAGAAIAAVA DEDADADAMP DVNYDPTLDL SRYQYPTLEL
LNDYGVAKAQ VTKEELEANK DRIVETLGHY GITIASIKAT IGPTVTLYEI VPEAGVRISK
IKSLEDDIAL SLAALGIRII APIPGKGTIG IEVPNAKKEM VSIRSVLGSE KFARTEMDLP
IAFGRTITNE VFVADLAKMP HLLMAGATGQ GKSVGLNVIL ASLLYKRHPA QLKFVLVDPK
KVELSIFNKI ERHYLAKLPD TNEPIITDTK KVVHTLNSLC MEMDRRYDLL KEAGCRNLKE
YNLKFVERRL NPKKGHRYLP FIVLVIDELA DLMMTAGKEV ETPIARLAQL ARAIGIHLIV
ATQRPSVNVI TGIIKANFPC RISFKVTSKI DSRTILDTGG ADQLIGQGDM LFSAGSDLIR
VQCAFIDTPE VDRVCDFISE QQGYSDAYLL PEVAGAEGDD GSGQDAGDPA ERDSMFEEAA
RCIVLHQQGS TSLLQRKLKL GYNRAGRLID QLQHAGIVGP FEGSKARDVL VPDEYQLEQL
LNSMPK
//
