ID A0A291QPK9_9BACT Unreviewed; 441 AA.
AC A0A291QPK9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cell division protein {ECO:0000313|EMBL:ATL45855.1};
GN ORFNames=COR50_01035 {ECO:0000313|EMBL:ATL45855.1};
OS Chitinophaga caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2029983 {ECO:0000313|EMBL:ATL45855.1, ECO:0000313|Proteomes:UP000220133};
RN [1] {ECO:0000313|EMBL:ATL45855.1, ECO:0000313|Proteomes:UP000220133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 {ECO:0000313|EMBL:ATL45855.1,
RC ECO:0000313|Proteomes:UP000220133};
RA Jin D., Kong X., Deng Y., Bai Z.;
RT "Paenichitinophaga pekingensis gen. nov., sp. nov., isolated from activated
RT sludge.";
RL Submitted (OCT-2017) 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; CP023777; ATL45855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291QPK9; -.
DR KEGG; cbae:COR50_01035; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000220133; 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 Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Cell cycle {ECO:0000313|EMBL:ATL45855.1};
KW Cell division {ECO:0000313|EMBL:ATL45855.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000220133};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 20..53
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 197..333
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 441 AA; 49913 MW; 4D1A03E3CA4DBCF0 CRC64;
MSTEVIKQLQ EAVAFSPNNV PLRVHLAQVL LQSFDYTQAE EQFRKALELD PQHEAAQLGL
ARTFFQQQKY TVAIVVLEQL EQQNPQHFDA LLLHCRILVK ENALREAKDI YQLLLDLNPQ
FRDEELDSKF RLTAQQPSFT GDDEEDMEDS QSAFMIEKPN MNFSDVGGME REKQEIELKI
IKPLQFPDLY KAYGKKAGGG ILLYGPPGCG KTYLAKATAG QINAEFISVG IHDILDMWVG
NSEKNLHALF ELARQNKPCV LFFDEVDALG ANRNTMKNNG SHLINQFLSE MDGITANNDD
ILIIGATNAP WHLDPAFRRP GRFDRIIFVE PPAQQGREEI LKIHLKGKPV DDIDYTSIAK
NTNGYSGADL KAIIDIATED KLLEALQTGK PQPITQKDLL KASKNHKATT REWFNTARNY
AMYSNESGIY NEVLKYLNIK K
//