ID A0A0H4VDW6_9SPHN Unreviewed; 768 AA.
AC A0A0H4VDW6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cell division cycle protein {ECO:0000313|EMBL:AKQ41279.1};
GN ORFNames=CP97_03325 {ECO:0000313|EMBL:AKQ41279.1};
OS Aurantiacibacter atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ41279.1, ECO:0000313|Proteomes:UP000059113};
RN [1] {ECO:0000313|EMBL:AKQ41279.1, ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RX PubMed=26220886; DOI=10.1099/ijsem.0.000481;
RA Zhuang L., Liu Y., Wang L., Wang W., Shao Z.;
RT "Erythrobacter atlanticus sp. nov., a bacterium from ocean sediment able to
RT degrade polycyclic aromatic hydrocarbons.";
RL Int. J. Syst. Evol. Microbiol. 65:3714-3719(2015).
RN [2] {ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RA Zhuang L., Liu Y., Shao Z.;
RT "The complete genome sequence of Erythrobacter sp. s21-N3.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CP011310; AKQ41279.1; -; Genomic_DNA.
DR RefSeq; WP_048884782.1; NZ_CP011310.1.
DR AlphaFoldDB; A0A0H4VDW6; -.
DR STRING; 1648404.CP97_03325; -.
DR KEGG; ery:CP97_03325; -.
DR PATRIC; fig|1648404.4.peg.702; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000059113; Chromosome.
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:0051301; P:cell division; 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; cd19503; RecA-like_CDC48_NLV2_r1-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
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; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01243; CDC48; 1.
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; 2.
DR Pfam; PF02933; CDC48_2; 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; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW Cell cycle {ECO:0000313|EMBL:AKQ41279.1};
KW Cell division {ECO:0000313|EMBL:AKQ41279.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000059113}.
FT DOMAIN 15..99
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 115..197
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 240..376
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 513..651
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 768 AA; 83709 MW; 0757A22C89665D60 CRC64;
MAEDDAGKIE AGTVRLQVAA ARQEESGRGI VRMPRSAFQA LGVTEGDAVE IEGKRVTVAQ
AATAYDEDEA LDVIRLDGLQ RGNAETSSGE HVMVRRAESK SATRVVFAPA RREMRLQGPT
EALKRVFFGK PLMTGDLVAT HGQQPVQNVP PEVRRMFNAP AYALTQIRLQ VVSTSPKGIV
QIDENTEIEL RAEFEEPRDA RGLINYDDVG GMEDTIKALR EMVELPLRYP ELFTRLGVDP
PKGVLLHGPP GTGKTRLAQA VANESDAEFF SIAGPEIMGS AYGESEKRLR EVFEEAERSQ
PAIIFIDEID SITPKREQTQ GEAEKRLVAQ LLTLMDGLQA RANLVVIAAT NRPDAIDEAL
RRPGRFDREI VIGVPDESGR REILAIHTRG MPMGDGVDLM ELSRSTHGFV GADLAALARE
AAIEAVRRIM PKIDLDAQEI PAEVLDELCV ERGDFREALK RVQPSAMREV MVQAPTVGWS
DLGGLDEAIN KLKEGVELPL KNPQAFDRLG IRPAKGFLLY GPPGTGKTLL AKAVAKEAEA
NFISMKSSDL LSKWFGESEQ QIARMFARAR AVAPCVIFID EIDSLVPARG SGAGEPQVTA
RVVNTILAEM DGMEDLSSIV VIGATNRPTL VDPALLRPGR FDELVYVGAP DAKGREHILK
IHTANMPLAG DVDLSTIAEK AERFTGADLE DVVRRAGLNA IRRSDGAPDV VTAADFAEAL
DDSRATVTAK MESEYSKMKG ELKRRAAEVR PIGFLTEGMV ESTRDQKH
//
