ID CDVC_SULAC Reviewed; 374 AA.
AC F2Z6D2;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Cell division protein C {ECO:0000305};
GN Name=cdvC {ECO:0000303|PubMed:18987308};
GN Synonyms=vps4 {ECO:0000303|PubMed:19008417};
GN OrderedLocusNames=Saci_1372 {ECO:0000312|EMBL:AAY80706.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=18987308; DOI=10.1073/pnas.0809467105;
RA Lindaas A.C., Karlsson E.A., Lindgren M.T., Ettema T.J., Bernander R.;
RT "A unique cell division machinery in the Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18942-18946(2008).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH CDVB, AND
RP DOMAIN.
RX PubMed=19008417; DOI=10.1126/science.1165322;
RA Samson R.Y., Obita T., Freund S.M., Williams R.L., Bell S.D.;
RT "A role for the ESCRT system in cell division in archaea.";
RL Science 322:1710-1713(2008).
CC -!- FUNCTION: Part of a cell division machinery (PubMed:18987308,
CC PubMed:19008417). The CdvA, CdvB and CdvC proteins polymerize between
CC segregating nucleoids and persist throughout cell division, forming a
CC successively smaller structure during constriction (PubMed:18987308).
CC {ECO:0000269|PubMed:18987308, ECO:0000269|PubMed:19008417}.
CC -!- SUBUNIT: Interacts with CdvB. {ECO:0000269|PubMed:19008417}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:18987308,
CC ECO:0000269|PubMed:19008417}. Note=Forms band-like structures between
CC segregating nucleoids (PubMed:18987308). Localizes to the mid-cell in
CC dividing cells (PubMed:19008417). {ECO:0000269|PubMed:18987308,
CC ECO:0000269|PubMed:19008417}.
CC -!- INDUCTION: Induced around the genome segregation and cell division
CC stages (PubMed:18987308). Down-regulated after UV irradiation,
CC indicating division inhibition in response to DNA damage
CC (PubMed:18987308). Expression is highest in dividing cells
CC (PubMed:19008417). {ECO:0000269|PubMed:18987308,
CC ECO:0000269|PubMed:19008417}.
CC -!- DOMAIN: The MIT domain is involved in interaction with CdvB.
CC {ECO:0000269|PubMed:19008417}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; CP000077; AAY80706.1; -; Genomic_DNA.
DR RefSeq; WP_011278208.1; NZ_CP046615.1.
DR AlphaFoldDB; F2Z6D2; -.
DR SMR; F2Z6D2; -.
DR STRING; 330779.Saci_1372; -.
DR TCDB; 3.A.31.1.3; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR GeneID; 78441718; -.
DR KEGG; sai:Saci_1372; -.
DR PATRIC; fig|330779.12.peg.1324; -.
DR eggNOG; arCOG01307; Archaea.
DR HOGENOM; CLU_000688_21_2_2; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd02682; MIT_AAA_Arch; 1.
DR CDD; cd19509; RecA-like_VPS4-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; NF041006; cell_div_CdvC; 1.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF83; VESICLE-FUSING ATPASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF04212; MIT; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..374
FT /note="Cell division protein C"
FT /id="PRO_0000438770"
FT DOMAIN 11..73
FT /note="MIT"
FT /evidence="ECO:0000255"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 374 AA; 42524 MW; 4D2413AFACCBA93B CRC64;
MSAQVMLEEM ARKYAINAVK ADKEGNAEEA ITNYKKAIEV LAQLVSLYRD GSTAAIYEQM
INEYKRRIEV LKELIPADGA GNGNGKHSQV SVDDLVMKEK PKVNFNDIVG LEDVKEALKE
AIVYPTRRPD LFPLGWPRGI LVYGPPGCGK TMIAAAVANE IDSYFIQVDA ASVMSKWLGE
AEKNVAKIFN SARELSKKDG KPVIIFIDEI DALLGTYNSE NGGEVRVRNQ FLKEMDGLQD
KSENFKVYVI GATNKPWRLD EPFLRRFQKR IYIRLPDIEQ RKSLLLHYTS KIKMDNVNID
ELAKMTEGYT ASDIKDIVQA AHIRVVKEMF DKKLEQPRAV NMEDFKEILK IRKPSVNSEV
IKVYEAWHEK YKAL
//
