ID   ZIPA_ECOLC              Reviewed;         328 AA.
AC   B1IX59;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   28-JAN-2026, entry version 89.
DE   RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   OrderedLocusNames=EcolC_1266;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 /
RC   Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein that stabilizes the FtsZ
CC       protofilaments by cross-linking them and that serves as a cytoplasmic
CC       membrane anchor for the Z ring. Also required for the recruitment to
CC       the septal ring of downstream cell division proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_00509}.
CC   -!- SUBUNIT: Interacts with FtsZ via their C-terminal domains.
CC       {ECO:0000255|HAMAP-Rule:MF_00509}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00509}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00509}. Note=Localizes to the Z ring in an FtsZ-dependent
CC       manner. {ECO:0000255|HAMAP-Rule:MF_00509}.
CC   -!- SIMILARITY: Belongs to the ZipA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00509}.
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DR   EMBL; CP000946; ACA76932.1; -; Genomic_DNA.
DR   RefSeq; WP_001300494.1; NC_010468.1.
DR   AlphaFoldDB; B1IX59; -.
DR   BMRB; B1IX59; -.
DR   SMR; B1IX59; -.
DR   KEGG; ecl:EcolC_1266; -.
DR   HOGENOM; CLU_030174_1_0_6; -.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000917; P:division septum assembly; IEA:TreeGrafter.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00231; ZipA; 1.
DR   FunFam; 3.30.1400.10:FF:000001; Cell division protein ZipA; 1.
DR   Gene3D; 3.30.1400.10; ZipA, C-terminal FtsZ-binding domain; 1.
DR   HAMAP; MF_00509; ZipA; 1.
DR   InterPro; IPR011919; Cell_div_ZipA.
DR   InterPro; IPR007449; ZipA_FtsZ-bd_C.
DR   InterPro; IPR036765; ZipA_FtsZ-bd_C_sf.
DR   NCBIfam; TIGR02205; septum_zipA; 1.
DR   PANTHER; PTHR38685; CELL DIVISION PROTEIN ZIPA; 1.
DR   PANTHER; PTHR38685:SF1; CELL DIVISION PROTEIN ZIPA; 1.
DR   Pfam; PF04354; ZipA_C; 1.
DR   SMART; SM00771; ZipA_C; 1.
DR   SUPFAM; SSF64383; Cell-division protein ZipA, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..328
FT                   /note="Cell division protein ZipA"
FT                   /id="PRO_1000081576"
FT   TOPO_DOM        1..6
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   TOPO_DOM        28..328
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   REGION          42..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..63
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..115
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..171
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  36475 MW;  A20F119A153A782B CRC64;
     MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD
     EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ PRQPVQQPPE AQVPPQHAPH
     PAQPVQQPAY QPQPEQPLQQ PVSPQVAPAP QPVHSAPQPA QQAFQPAEPV AAPQPEPVAE
     PAPVMDKPKR KEAVIIMNVA AHHGSELNGE LLLNSIQQAG FIFGDMNIYH RHLSPDGSGP
     ALFSLANMVK PGTFDPEMKD FTTPGVTIFM QVPSYGDELQ NFKLMLQSAQ HIADEVGGVV
     LDDQRRMMTP QKLREYQDII REVKDANA
//