ID A0A0A2UTT0_9BACI Unreviewed; 1035 AA.
AC A0A0A2UTT0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Stage III sporulation protein E {ECO:0000313|EMBL:KGP90183.1};
GN ORFNames=N780_06440 {ECO:0000313|EMBL:KGP90183.1};
OS Pontibacillus chungwhensis BH030062.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385513 {ECO:0000313|EMBL:KGP90183.1, ECO:0000313|Proteomes:UP000030153};
RN [1] {ECO:0000313|EMBL:KGP90183.1, ECO:0000313|Proteomes:UP000030153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030062 {ECO:0000313|EMBL:KGP90183.1,
RC ECO:0000313|Proteomes:UP000030153};
RA Wang Q., Wang G.;
RT "Genome of Pontibacillus chungwhensis.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:KGP90183.1}.
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; AVBG01000015; KGP90183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2UTT0; -.
DR STRING; 1385513.N780_06440; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000030153; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; 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; IPR003593; AAA+_ATPase.
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:SF42; DNA TRANSLOCASE SFTA; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00382; AAA; 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}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000030153}.
FT DOMAIN 699..891
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 716..723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1035 AA; 117240 MW; DAC5DBE9AB9143CA CRC64;
MWNRMKNWLH QMRQEEQSPE DQQPPFPQED ETKHQKQQGQ QTQQQFQTKM VYQYPKQGNF
RFPMIPDSQQ KREPRQRNTD SKNEQSNRTQ SQRSNYDSYK YSNAKQNKEW GKKDTYQPSS
FEQGSPFTPS NVPSPIYGYG KREGHFSETV LDDLPSVMKK ADEDDRLYES TLAKVLPETH
PSKSMIPPKQ EEEEERVSVS EEQVDEEVEE PEEDNVIGLF NHEDPIESSH EVEYFSDQED
EEEDDEDVPP TIIMYGSRDT EPDSPDEETL SSEKVADDPS VENEEGTVKD ETASNSEKGY
LPPSMLEMDE SYEEEGVSVV DEEFSYQDEH ATEEAVNGFE MGKTTSSAEE KDENEGKPDG
DAYSEEPETT VEEQLENSSD LNEVYTVDET FDTDEAEGSL NETVTFKDEF EEDPEDVENL
ELETNEVHPV NGTSDSDESE KMVADQSLEE EPLQQIQELS YEGKGTGETK EETTNSENES
GAEEQIAATQ VKDEGNLETK PTEPERPKRR SRPFNVIMTP RDKRHRDQQK AVTSTQPKQV
EKPPKKEEVV EEKEETKEKA PTQSTIPPYH LLNDPPKRME SEDEWIEEQM QLLETTLHNF
HVKAKVVNAM KGPAVTRFEV QPEPGVKVSK ITNLSDDIKM SLAAKDIRME APIPGKNAIG
IEVPNQKSEA VGLQEILESD AFQGESSPLS VGLGLDIEGS PIVTDLKKMP HGLIAGATGS
GKSVCINTIL LSLLYKASHE DVKFLLIDPK MVELAPYNEL PHLVAPVITD VKAATSALKW
AVKEMEQRYE RFVEEGVRDI DRYNDKIKAK GRLNDKMPYL VIVIDELADL MMMSPQDVED
AICRIAQKAR ACGIHLLLAT QRPSVDVITG LIKANIPTRV AFSVSSQVDS RTIVDSAGAE
KLLGRGDMLF LENGAGKTKR IQGAFVSDEE IERITNHVKK IASPNYLFEQ EELMQQPNFE
ETEDDLFEEA VQFVIDQNGA SASLLQRRFK VGYNRAARLI DTMEEKGIIS ESKGSKPRDV
YMDHAGFEEL RRDHE
//
