ZIPA_SERP5
ID ZIPA_SERP5 Reviewed; 332 AA.
AC A8GHF3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=Spro_3445;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) 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; CP000826; ABV42543.1; -; Genomic_DNA.
DR RefSeq; WP_012146158.1; NC_009832.1.
DR AlphaFoldDB; A8GHF3; -.
DR SMR; A8GHF3; -.
DR STRING; 399741.Spro_3445; -.
DR EnsemblBacteria; ABV42543; ABV42543; Spro_3445.
DR KEGG; spe:Spro_3445; -.
DR eggNOG; COG3115; Bacteria.
DR HOGENOM; CLU_030174_1_0_6; -.
DR OMA; FWSIRKQ; -.
DR OrthoDB; 1632200at2; -.
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..332
FT /note="Cell division protein ZipA"
FT /id="PRO_1000060870"
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 34..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 36429 MW; 5B9380F53F7FC32E CRC64;
MMQDLRLILI VVGAIAIIAL LLHGLWTSRK ERSSLFRDRP AKRSKKEREQ SPIDELDEGV
GEVRVRSAHP EDEPSFGHFD AAREEPVVAP KPAPAAEPAP RAVQPAAHQT PPPLSQRPDY
DDILLDNYAQ EEDDEPQQPA PRREPRVDDL PPVAPAAEPA FHAEPAHQPQ PEVKPAVAHE
PQPAPAAIKP AKLKETVLVL HVTAHQGGVI GGEILLQSVL QAGFQFGEMG IFHRHISPAG
SGPVLFSLAN MVKPGSFDPE MMSDFSTPGV SMFMMVPSYG DANQNFKLML QSAQRIADDV
GGVVLDDERR MMTPQKLETY KARLREVLEN NA