ID A0A0C2PZ11_9CYAN Unreviewed; 650 AA.
AC A0A0C2PZ11;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KIJ73298.1};
DE Flags: Fragment;
GN ORFNames=SD81_34330 {ECO:0000313|EMBL:KIJ73298.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ73298.1};
RN [1] {ECO:0000313|EMBL:KIJ73298.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ73298.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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:KIJ73298.1}.
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DR EMBL; JXCB01000013; KIJ73298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2PZ11; -.
DR OrthoDB; 9807790at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:0000313|EMBL:KIJ73298.1};
KW Cell division {ECO:0000313|EMBL:KIJ73298.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 359..552
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 627..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT NON_TER 650
FT /evidence="ECO:0000313|EMBL:KIJ73298.1"
SQ SEQUENCE 650 AA; 73189 MW; 4BE9B6059C1EB634 CRC64;
MLVPYNNNIE SQKQQVLTAI VQAKQDGLSN EEIMVNVWRA LPSLVSYAET VLQQIDFKTK
LSRPVVEFDL EFLFQLIYES VIALTSDEEI LSVCAEHCTL NQYEFVRYAL EYIHVNRVPS
QWEQSNIHYK IVQIADSCPM ESLFEYIDSI KNIYLKQIGY QVVQENLYSL FLSNKQVSYF
LELVNKTKDD FIKNYCYRTA VLVARVTGKP IDLQLTGDGS TINEPKSLDS KAATNKIIHS
QISTMEQAGK LLVDTLEDFS INAKYVDAKT GPTFNRIKVK LGRGVTYKKV EDIGNDLVQQ
LGEELGLKVA PMVSVVTGGV VFDIPRLDRQ FAYFRDYVRF NGEPDIHSVS IPGGVDVDGT
YVEIPLYSDN VTHILGGGRT RGGKSQFEKA AILYLVRRYP PSVVRLALSD VKRVTFGKFD
GLPHLIAPVA RDAESTANLL DYLVEEMELR YQEFEQHSSI ETIAQYNLRF APGIVMPRLV
CLIDECFDLL SDDKYCSRIE SALMKLLAKA GGAGIHVLLY TQRPDKNVID PLIRSNFPAK
TAFVTTRPED SCIILGDDKD KRAVYLLGYG DFLYKTTEVV RLQALYVADD EDPEYFKQLL
IDAKNQNGSY TAWESGLDFD EFVASLSGEG SSHDSGKSKA TAVTKTKQSK
//
