ZIPA_SHISS
ID ZIPA_SHISS Reviewed; 328 AA.
AC Q3YZD0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=SSON_2501;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ89132.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZD0; -.
DR SMR; Q3YZD0; -.
DR EnsemblBacteria; AAZ89132; AAZ89132; SSON_2501.
DR KEGG; ssn:SSON_2501; -.
DR HOGENOM; CLU_030174_1_0_6; -.
DR OMA; FWSIRKQ; -.
DR Proteomes; UP000002529; 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..328
FT /note="Cell division protein ZipA"
FT /id="PRO_0000237137"
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 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 328 AA; 36540 MW; A3DCAABCFCF2F463 CRC64;
MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD
EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ PRQPIQQPPE AQVPPQHAPR
PAQPMQQPAY QPQPEQPLQQ PVSPQVAPAP QPVHSAPQPA QQAFQPAEPV AAPQPEPVAE
PAPVMDKPKR KEAVIIMNVA AHHGSELNGE LLLNSIQQAG FIFGDMNIYH RHLSPDGSGP
ALFSLANMVK PGTFDPEMKD FTTPGVTIFM QVPSYGDELQ NFKLMLQSAQ HIADEVGGVV
LDDQRRMMTP QKLREYQDII REVKDANA