ID H5V5J9_ATLHE Unreviewed; 374 AA.
AC H5V5J9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=yhcM {ECO:0000313|EMBL:GAB53257.1};
GN Synonyms=zapE {ECO:0000256|HAMAP-Rule:MF_01919};
GN ORFNames=EH105704_13_00440 {ECO:0000313|EMBL:GAB53257.1};
OS Atlantibacter hermannii NBRC 105704.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Atlantibacter.
OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB53257.1, ECO:0000313|Proteomes:UP000010297};
RN [1] {ECO:0000313|EMBL:GAB53257.1, ECO:0000313|Proteomes:UP000010297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB53257.1,
RC ECO:0000313|Proteomes:UP000010297};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:GAB53257.1}.
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DR EMBL; BAFF01000013; GAB53257.1; -; Genomic_DNA.
DR RefSeq; WP_002437468.1; NZ_BAFF01000013.1.
DR AlphaFoldDB; H5V5J9; -.
DR eggNOG; COG1485; Bacteria.
DR Proteomes; UP000010297; Unassembled WGS sequence.
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:UP000010297}.
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 374 AA; 42952 MW; EFBBA12611FE4798 CRC64;
MQNLSPTSRY LQALQDKSHQ PDDVQREAVN RLEAIYQALT AKRDEPPQEQ GLKAAFTKLL
GKRPSAPSTP VRGLYMWGGV GRGKTWLMDL FYQSLPGERK QRLHFHRFML HVHEELGQLQ
GQTDPLEIIA DRFKAKTDVL CFDEFFVSDI TDAMLLGGLM KALFSRGITL VATSNIPPDE
LYRNGLQRTR FLPAIEAIKH YCDVMNVDAG IDYRLRTLTQ AHLWLSPLNE ETRQQMDALW
RALAGGSREN APTLEINHRP LATLGVENQT LAVSFSTLCV DARSQHDYIE LSRQFHTVML
HDVAVMTKLN ENEARRFIAL VDEFYERRVK LVVTAAAPMF EIYAGEQLKF EFQRCLSRLQ
EMQSEEYLRS EHMP
//