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Database: UniProt
Entry: E3G4A1_ENTLS
LinkDB: E3G4A1_ENTLS
Original site: E3G4A1_ENTLS 
ID   E3G4A1_ENTLS            Unreviewed;       109 AA.
AC   E3G4A1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Cell division protein ZapA {ECO:0000256|ARBA:ARBA00015195, ECO:0000256|HAMAP-Rule:MF_02012};
DE   AltName: Full=Z ring-associated protein ZapA {ECO:0000256|ARBA:ARBA00033158, ECO:0000256|HAMAP-Rule:MF_02012};
GN   Name=zapA {ECO:0000256|HAMAP-Rule:MF_02012};
GN   OrderedLocusNames=Entcl_0842 {ECO:0000313|EMBL:ADO47116.1};
OS   Enterobacter lignolyticus (strain SCF1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO47116.1, ECO:0000313|Proteomes:UP000006872};
RN   [1] {ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA   Hazen T.C., Woyke T.;
RT   "Complete sequence of Enterobacter cloacae SCF1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO47116.1, ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|EMBL:ADO47116.1,
RC   ECO:0000313|Proteomes:UP000006872};
RX   PubMed=22180812; DOI=10.4056/sigs.2104875;
RA   Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA   Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA   Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT   "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL   Stand. Genomic Sci. 5:69-85(2011).
CC   -!- FUNCTION: Activator of cell division through the inhibition of FtsZ
CC       GTPase activity, therefore promoting FtsZ assembly into bundles of
CC       protofilaments necessary for the formation of the division Z ring. It
CC       is recruited early at mid-cell but it is not essential for cell
CC       division. {ECO:0000256|ARBA:ARBA00024910, ECO:0000256|HAMAP-
CC       Rule:MF_02012}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ.
CC       {ECO:0000256|ARBA:ARBA00026068, ECO:0000256|HAMAP-Rule:MF_02012}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02012}.
CC       Note=Localizes at mid-cell. {ECO:0000256|HAMAP-Rule:MF_02012}.
CC   -!- SIMILARITY: Belongs to the ZapA family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010074, ECO:0000256|HAMAP-Rule:MF_02012}.
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DR   EMBL; CP002272; ADO47116.1; -; Genomic_DNA.
DR   RefSeq; WP_013364868.1; NC_014618.1.
DR   AlphaFoldDB; E3G4A1; -.
DR   STRING; 701347.Entcl_0842; -.
DR   KEGG; esc:Entcl_0842; -.
DR   eggNOG; COG3027; Bacteria.
DR   HOGENOM; CLU_116623_3_0_6; -.
DR   Proteomes; UP000006872; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.50; -; 1.
DR   Gene3D; 3.30.160.880; Cell division protein ZapA protomer, N-terminal domain; 1.
DR   HAMAP; MF_02012; ZapA_type1; 1.
DR   InterPro; IPR007838; Cell_div_ZapA-like.
DR   InterPro; IPR036192; Cell_div_ZapA-like_sf.
DR   InterPro; IPR023771; Cell_div_ZapA_eubact.
DR   InterPro; IPR042233; Cell_div_ZapA_N.
DR   PANTHER; PTHR34981; CELL DIVISION PROTEIN ZAPA; 1.
DR   PANTHER; PTHR34981:SF1; CELL DIVISION PROTEIN ZAPA; 1.
DR   Pfam; PF05164; ZapA; 1.
DR   SUPFAM; SSF102829; Cell division protein ZapA-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02012};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02012}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02012};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006872};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_02012}.
FT   COILED          24..51
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02012"
SQ   SEQUENCE   109 AA;  12622 MW;  805EC93E0F975279 CRC64;
     MSAQPVDIQI FGRSLRVNCP PEQRDALNQA ADDLNQRLQD LKERTRVTNT EQLVFIAALN
     ISYELTQERA KTRDYASSME QRIRMLQQTI EQALLDQGRI TERTGPKFE
//
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