ID   ZIPA_SHEFN              Reviewed;         352 AA.
AC   Q080K8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=Sfri_2462;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI72307.1; -; Genomic_DNA.
DR   RefSeq; WP_011637916.1; NC_008345.1.
DR   AlphaFoldDB; Q080K8; -.
DR   SMR; Q080K8; -.
DR   STRING; 318167.Sfri_2462; -.
DR   EnsemblBacteria; ABI72307; ABI72307; Sfri_2462.
DR   KEGG; sfr:Sfri_2462; -.
DR   eggNOG; COG3115; Bacteria.
DR   HOGENOM; CLU_030174_1_0_6; -.
DR   OMA; FWSIRKQ; -.
DR   OrthoDB; 1632200at2; -.
DR   Proteomes; UP000000684; 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   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..352
FT                   /note="Cell division protein ZipA"
FT                   /id="PRO_1000015155"
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..352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   REGION          78..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  38620 MW;  6F53957E84F5E471 CRC64;
     MKDLQLVLFV LGAIAIIAVL VHGFWSIRKQ QPKSMKQSPM AGFYKDQAKR RDSEGFDADG
     IGQVRVRKPG EVEETVIKPV LKTNLSQKPH SGTTKLTDTP LQDSLRQPGP HKTEPEHVEP
     KVVQPAQQSL FVGDDVKPAP TASTSMNTPK KIFNPSTSTA KLESYTGKPV AARPEPIKPP
     IQPAAPKVDV KAEVEEVKAE VEVKSTLKAD APVNEPVEPT DVLVLHIFAK AGEQIQGAEL
     LPSLLSLNFK FGDMDIFHRH IDNAGTGKVL FSLANMLKPG IFDPDNMEQF VTQGVVLFMT
     LPGYGDPLMN FTIMLNSAYQ IAEDLGAELL DGQRQPWSDA TKKDYLRRLN AA