ID A0A0A0BM52_9CELL Unreviewed; 662 AA.
AC A0A0A0BM52;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Cell division protein FtsH {ECO:0000313|EMBL:KGM08985.1};
GN ORFNames=N868_05120 {ECO:0000313|EMBL:KGM08985.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM08985.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM08985.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM08985.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM08985.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM08985.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
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:KGM08985.1}.
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DR EMBL; AXCY01000133; KGM08985.1; -; Genomic_DNA.
DR RefSeq; WP_052426524.1; NZ_AXCY01000133.1.
DR AlphaFoldDB; A0A0A0BM52; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000029839; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
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:KGM08985.1};
KW Cell division {ECO:0000313|EMBL:KGM08985.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029839};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 258..397
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 69029 MW; FC35AA65A5FD8BA3 CRC64;
MNPEDLTNPA RTSATEPSAV DVRAGQLTDQ LTDQLREHHG AEPRTIEHTG DPASRPGGGS
SGAAKERAFR LGPRPTRRQA LVAAVVVLLA VGGAVTAGWL TRAPAVEEVT LTQALGLIEA
GDVTAATLDD ASATVTLTLA RGDVRAAYPA AYADELTTRL VDEDVPLATA AGGSDLGRDA
LMTLGPLVLI LGVLVWAVRK ASPAGAFGGA KKKALTSGEV PEVTFADVAG ADEAVDQLRE
MVQFLREPER FEAVGARRPR GALLVGPPGT GKTLLARAVA GEAGVPFFAL AGSDFVETFV
GVGARRVRDL FAEARKAERA IIFIDEIDAV GRTRSGAATN GGEGERENTL ISLLNEMDGF
AGSSIIVLAA TNRPDILDSA LTRPGRLDRQ VHVPNPDRRG RTLILQVHAR SKPVADDVDL
VQIARQTPGM SGADLAAVVN EACMEAARRG ATLVDASCFQ AAVATVAMGR ARTSALVTDF
DRRVTAWHEA GHTVAAALLP DADDPVSVTI VPRGPAGGVT WMSGNDDIFL PKKKALAQLV
VAMAGRAAEE RLLDGEHTQG AMGDLQHATG LATAMVTKYG MTEFGYAQVD DDTLRVGGQV
AAQAHAQVDA LLRDAHATAT ALVAENAEVL DAVAEALLVE ETLSVGRVRQ IVEETRSRAV
AA
//
