ID A4T2V8_MYCGI Unreviewed; 729 AA.
AC A4T2V8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Vesicle-fusing ATPase {ECO:0000313|EMBL:ABP42650.1};
DE EC=3.6.4.6 {ECO:0000313|EMBL:ABP42650.1};
GN OrderedLocusNames=Mflv_0155 {ECO:0000313|EMBL:ABP42650.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP42650.1};
RN [1] {ECO:0000313|EMBL:ABP42650.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP42650.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP42650.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP42650.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CP000656; ABP42650.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T2V8; -.
DR STRING; 350054.Mflv_0155; -.
DR KEGG; mgi:Mflv_0155; -.
DR eggNOG; COG0464; Bacteria.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_000688_12_3_11; -.
DR OrthoDB; 9809379at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd19511; RecA-like_CDC48_r2-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000313|EMBL:ABP42650.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651}.
FT DOMAIN 5..89
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 106..188
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 252..377
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 502..639
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 189..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 75840 MW; 42A3883E6C10DF9F CRC64;
MAQLTLTARL NTSALDSRRG VVRLHPEAIA ALGIREWDAV SLTGARTTAA VVGIAPAGTP
TGTALLDDVT LSNAGLREDT SVLVSDVTVY GARSVTLSGS RLASRSITPA TLRQALLGKV
MTVGDTVSLL PRDLGPGTST STASAALASS VGITWTSELL TVTAADPIGP VSVQPNSLVC
WASGASEASG TSEAANGTSE VSGAPVRTEQ PRTQAVGFDD LKGAHAQAGR LTEWLKLALD
QPELLEKLGA TANLGVLVSG PAGVGKATLV RTVCAERRLI ELDGPEVGSL RADDRLAAVS
SAAASARDGG GVLLVTDIDA LLPVPPDPVA TLILTELRSA VAGGVVFVAT SAVPDNVDPR
LRAPDLCDRE LGLSLPDGAV RKQLLEVLLR DVPSANLEIG EITDRTPGFV VADLAALVRE
AALRAAARAS ENGEPPALRQ EDLVGALGVI RPLSRSATEE VSVGAVTLDD VGDMAETKQA
LTEAVLWPLQ HPETFQRLGV EPPRGVLLYG PPGCGKTFVV RALASSGRLS VHAVKGAELM
DKWVGSSEKA VRELFQRARD SAPSLVFLDE IDALAPRRGQ SFDSGVTDRV VAAMLTELDG
IEPLRDVVVL GATNRPDLID PALLRPGRLE KLVFVEPPDA EARTQILRTA GKSVPLAADV
DLEVLAADLD GYSAADCVAL LREAALTAMR RSIDAADVTA DDVARARETV RPSLDPAQVE
SLRQFADTR
//
