ID A0A1G2MXV1_9BACT Unreviewed; 617 AA.
AC A0A1G2MXV1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cell division protein FtsH {ECO:0000313|EMBL:OHA28755.1};
DE Flags: Fragment;
GN ORFNames=A3F51_00005 {ECO:0000313|EMBL:OHA28755.1};
OS Candidatus Taylorbacteria bacterium RIFCSPHIGHO2_12_FULL_45_16.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802315 {ECO:0000313|EMBL:OHA28755.1, ECO:0000313|Proteomes:UP000178089};
RN [1] {ECO:0000313|EMBL:OHA28755.1, ECO:0000313|Proteomes:UP000178089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
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:OHA28755.1}.
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DR EMBL; MHRT01000009; OHA28755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2MXV1; -.
DR STRING; 1802315.A3F51_00005; -.
DR Proteomes; UP000178089; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Cell cycle {ECO:0000313|EMBL:OHA28755.1};
KW Cell division {ECO:0000313|EMBL:OHA28755.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 104..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..333
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OHA28755.1"
SQ SEQUENCE 617 AA; 67800 MW; 1B7894B418D0CBE2 CRC64;
LLSRNLIIGF LILMLLAGAY SVFLESFKEV PSLSLSDLVK KINAGEVKSI SINGDDLNVT
LGDESAFIAK KESESSLLQT LSNYGVSKEA LDKVAINIDS PSGLVFWLSA ILPFLLPFLL
IVLFFWLAAR QVQRSNVQAF TFGQSRARVV QPDSKKERVT FKDVAGVKEA KEELQEIVEF
LRSPRKFLDI GARIPKGVLL MGAPGTGKTL LARAVAGEAG VPFFHMSGSE FVEMFVGVGA
SRVRDLFKMA KRSAPAIIFI DEIDAVGRHR GAGMGGGHDE REQTLNQILV EMDGFEQQES
VIVMAGTNRP DVLDPALLRP GRFDRRVILD NPDINDREAI LKLHAQKKPL EKEVDLRVIA
ERTPGFSGAD LANLMNEAAI VAARDNRKTI EQLDLFRSIE KVLLGPERKS HILSTAEKKI
SAYHEAGHAL VAAILPNADP VHKTTIVSRG RAAGYTLKLP SEDRHLYSRK NFLDELAAAL
GGYASEKLVF GELTTGSSDD IKKATLIARD LVTRYGMSEK IGPITLGERD ELVFLGKELG
VEKNYSEATA QLVDSEVAHI MRNAFKRAND VLKKYRKVLD SLASHLIKNE TIEREEFDSI
LATFGLAQVI GKQAEAV
//
