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   03-AUG-2022, entry version 54.
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; Crenarchaeota; 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; NC_007181.1.
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   EnsemblBacteria; AAY80706; AAY80706; Saci_1372.
DR   GeneID; 3472937; -.
DR   KEGG; sai:Saci_1372; -.
DR   PATRIC; fig|330779.12.peg.1324; -.
DR   eggNOG; arCOG01307; Archaea.
DR   HOGENOM; CLU_000688_21_2_2; -.
DR   OMA; ATIMSKW; -.
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   Gene3D; 3.40.50.300; -; 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   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; SSF116846; 1.
DR   SUPFAM; SSF52540; SSF52540; 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