ID   ZIPA_PECAS              Reviewed;         332 AA.
AC   Q6D8S6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=ECA0896;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73808.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6D8S6; -.
DR   SMR; Q6D8S6; -.
DR   STRING; 218491.ECA0896; -.
DR   EnsemblBacteria; CAG73808; CAG73808; ECA0896.
DR   KEGG; eca:ECA0896; -.
DR   eggNOG; COG3115; Bacteria.
DR   HOGENOM; CLU_030174_1_0_6; -.
DR   OMA; FWSIRKQ; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0090529; P:cell septum assembly; IEA:InterPro.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00231; ZipA; 1.
DR   Gene3D; 3.30.1400.10; -; 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   PANTHER; PTHR38685; PTHR38685; 1.
DR   Pfam; PF04354; ZipA_C; 1.
DR   SMART; SM00771; ZipA_C; 1.
DR   SUPFAM; SSF64383; SSF64383; 1.
DR   TIGRFAMs; TIGR02205; septum_zipA; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..332
FT                   /note="Cell division protein ZipA"
FT                   /id="PRO_0000214524"
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..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   REGION          40..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  36237 MW;  9100C81DCC462B96 CRC64;
     MMQDLRLILI VVGAIAIIAL LLHGLWTSRK ERSSLFRDRP VKRAKKARDE TPLDDLDEGV
     GEVRVKGARP QQSEPSFDSA SVDSSSFDNY GSAREDVRSE AKSPFEHMSP VSAYDPLLDE
     ATPVDSPRSQ VRGDANPQVV DPRQAFIPES DIDAPREPFA YDAPSSAQQQ PVSHSLHEKV
     QPAPQQPAEP AAAKETVLVL HVVAHQGGVI GGELLLQSLL QAGFQFGEMN IFHRHVNPAG
     AGPVLFSLAN MVKPGSFNVD TMSEFSTPGV SIFMMVPSYG DAGQNFKLML QSAQRIADDV
     GGVVQDDERR MMTPQKVESY KARIRDVLKA NA