ID U5T5A5_9GAMM Unreviewed; 366 AA.
AC U5T5A5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Cell division protein ZapE {ECO:0000256|HAMAP-Rule:MF_01919};
DE AltName: Full=Z ring-associated protein ZapE {ECO:0000256|HAMAP-Rule:MF_01919};
GN Name=zapE {ECO:0000256|HAMAP-Rule:MF_01919};
GN ORFNames=SPICUR_01665 {ECO:0000313|EMBL:AGY91352.1};
OS Spiribacter curvatus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=1335757 {ECO:0000313|EMBL:AGY91352.1, ECO:0000313|Proteomes:UP000017640};
RN [1] {ECO:0000313|EMBL:AGY91352.1, ECO:0000313|Proteomes:UP000017640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAH-SP71 {ECO:0000313|EMBL:AGY91352.1,
RC ECO:0000313|Proteomes:UP000017640};
RX PubMed=24225341; DOI=10.1186/1471-2164-14-787;
RA Lopez-Perez M., Ghai R., Leon M.J., Rodriguez-Olmos A., Copa-Patino J.L.,
RA Soliveri J., Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "Genomes of "Spiribacter", a streamlined, successful halophilic
RT bacterium.";
RL BMC Genomics 14:787-787(2013).
CC -!- FUNCTION: Reduces the stability of FtsZ polymers in the presence of
CC ATP. {ECO:0000256|HAMAP-Rule:MF_01919}.
CC -!- SUBUNIT: Interacts with FtsZ. {ECO:0000256|HAMAP-Rule:MF_01919}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01919}.
CC -!- SIMILARITY: Belongs to the AFG1 ATPase family. ZapE subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01919}.
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DR EMBL; CP005990; AGY91352.1; -; Genomic_DNA.
DR AlphaFoldDB; U5T5A5; -.
DR STRING; 1335757.SPICUR_01665; -.
DR KEGG; spiu:SPICUR_01665; -.
DR PATRIC; fig|1335757.3.peg.328; -.
DR eggNOG; COG1485; Bacteria.
DR HOGENOM; CLU_008681_0_4_6; -.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000017640; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01919; ZapE; 1.
DR InterPro; IPR005654; ATPase_AFG1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030870; ZapE.
DR NCBIfam; NF040713; ZapE; 1.
DR PANTHER; PTHR12169:SF6; AFG1-LIKE ATPASE; 1.
DR PANTHER; PTHR12169; ATPASE N2B; 1.
DR Pfam; PF03969; AFG1_ATPase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01919}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_01919};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_01919};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01919};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01919};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01919}; Reference proteome {ECO:0000313|Proteomes:UP000017640}.
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 366 AA; 41858 MW; 699D01657890A4E9 CRC64;
MTTPSSRYEA DLAGGDFVDD EAQRAAVEAL DALHASLLAQ PPRPTGWRGW WRRRRGESSD
AIPGLYLWGG VGRGKTYLMD TFYECLPASI GKRRVHFHRF MQSAHQRLRW LREQPDPLRS
LAAEWAADLR VLCFDEFFVS DIGDAMILSG LLHGLIEEGV TLVATSNIAP AGLYEDGLQR
DRFLPAIDLL ERHLQVINVD GGLDYRLRLL SRAPIYHVPA DDRAEAALAK TFERMCPERD
HDTPELSINQ RDIPVRALGD GVLWCRFADL CEGPRSADDY VEIARRFHTV ILSGLPILDR
EREDAARRFA SLVDEFYDRG VKLIISATAD VEWLYRGRHL HFEFRRIVSR LQEMRSHEYL
AMPHRP
//
