ID A0A162PAN2_9BACT Unreviewed; 433 AA.
AC A0A162PAN2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Cell division protein {ECO:0000313|EMBL:KYP14265.1};
GN ORFNames=A1D16_17615 {ECO:0000313|EMBL:KYP14265.1};
OS Flavihumibacter sp. CACIAM 22H1.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1812911 {ECO:0000313|EMBL:KYP14265.1, ECO:0000313|Proteomes:UP000075747};
RN [1] {ECO:0000313|EMBL:KYP14265.1, ECO:0000313|Proteomes:UP000075747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIAM 22H1 {ECO:0000313|EMBL:KYP14265.1};
RA Moraes P.G., Lima A.R.;
RT "Draft Genome of Flavihumibacter sp. CACIAM 22H1.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYP14265.1}.
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DR EMBL; LUKG01000047; KYP14265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162PAN2; -.
DR STRING; 1812911.A1D16_17615; -.
DR Proteomes; UP000075747; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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 PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Cell cycle {ECO:0000313|EMBL:KYP14265.1};
KW Cell division {ECO:0000313|EMBL:KYP14265.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651}.
FT DOMAIN 188..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 22..53
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 433 AA; 48518 MW; 45EC6C40A2FB6B3A CRC64;
MDEQMIESLR QALAVSPENI PLKLHLAQVL HQANRLEEAE KEYTELMRLT RDEKPRIGLA
RIFFAQGAYS KCNVILEQLL QDSNELEYLL LHSRALLREK RIADAMQVYE QVLHLQPNFQ
DEELDKALRV SGAMVTEEDS DFAGHTVQRP TVGFQDVGGM DGVKKEIELK IIKPLLHPEL
YKAYGKKIGG GILLYGPPGC GKTFIARATA GQVNAQFISV GLNDILDMWI GNSEKNLHQV
FEIARQNTPC VLFIDEIDAL GASRSDMKQS AGRHLINQFL LELDGIDYSN EGILIIGATN
TPWHLDTAFR RPGRFDRILF IPPPDESARA SILRLKLANK PVASVDYEAV AKKLEHYSGA
DIEAVIDLAI EEKLDAAFTT GIPEPISTKD LLQAARKHKP STQEWFSKAK NFALFANEGG
LYDDILSYLK IKK
//
