ID   ZAPD_VIBPA              Reviewed;         246 AA.
AC   Q87LT3;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Cell division protein ZapD {ECO:0000255|HAMAP-Rule:MF_01092};
DE   AltName: Full=Z ring-associated protein D {ECO:0000255|HAMAP-Rule:MF_01092};
GN   Name=zapD {ECO:0000255|HAMAP-Rule:MF_01092}; OrderedLocusNames=VP2528;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 2-245.
RC   STRAIN=RIMD 2210633;
RG   Midwest center for structural genomics (MCSG);
RT   "Crystal structure of the protein of unknown function VP2528 from Vibrio
RT   parahaemolyticus.";
RL   Submitted (JUL-2011) to the PDB data bank.
CC   -!- FUNCTION: Cell division factor that enhances FtsZ-ring assembly.
CC       Directly interacts with FtsZ and promotes bundling of FtsZ
CC       protofilaments, with a reduction in FtsZ GTPase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01092}.
CC   -!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01092}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01092}.
CC       Note=Localizes to mid-cell in an FtsZ-dependent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_01092}.
CC   -!- SIMILARITY: Belongs to the ZapD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01092}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000031; BAC60791.1; -; Genomic_DNA.
DR   RefSeq; NP_798907.1; NC_004603.1.
DR   RefSeq; WP_005480890.1; NC_004603.1.
DR   PDB; 2OEZ; X-ray; 1.97 A; A/B=2-245.
DR   PDBsum; 2OEZ; -.
DR   AlphaFoldDB; Q87LT3; -.
DR   SMR; Q87LT3; -.
DR   STRING; 223926.28807526; -.
DR   EnsemblBacteria; BAC60791; BAC60791; BAC60791.
DR   GeneID; 1190043; -.
DR   KEGG; vpa:VP2528; -.
DR   PATRIC; fig|223926.6.peg.2425; -.
DR   eggNOG; COG4582; Bacteria.
DR   HOGENOM; CLU_076303_0_0_6; -.
DR   OMA; LPAYYAW; -.
DR   EvolutionaryTrace; Q87LT3; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.440.10; -; 1.
DR   HAMAP; MF_01092; ZapD; 1.
DR   InterPro; IPR009777; ZapD.
DR   InterPro; IPR027462; ZapD_C.
DR   InterPro; IPR036268; ZapD_sf.
DR   PANTHER; PTHR39455; PTHR39455; 1.
DR   Pfam; PF07072; ZapD; 1.
DR   SUPFAM; SSF160950; SSF160950; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; Reference proteome;
KW   Septation.
FT   CHAIN           1..246
FT                   /note="Cell division protein ZapD"
FT                   /id="PRO_0000211684"
FT   STRAND          3..11
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           12..30
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           38..55
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           58..74
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   TURN            75..78
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           84..103
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           109..113
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           115..125
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           146..158
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           161..176
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          199..205
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          220..227
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   TURN            228..230
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:2OEZ"
FT   STRAND          238..245
FT                   /evidence="ECO:0007829|PDB:2OEZ"
SQ   SEQUENCE   246 AA;  28621 MW;  749309A376A04321 CRC64;
     MTTHKFEHPL NEKTRIYLRV ESLLRQAHLA SGFADNHQYQ LFFRALFDMV EIFEQIQLKS
     ELAKDLEKQR LSYRHWLNVE GVDQEALNSL LNEIDVVHSQ LMGAERFGQA LKEDRFLSSI
     RQRFNLPGGS CCFDLPALHY WLHLPIERKK HDANQWQKSL KPLSDALTLW LKLARETGHF
     KAQIARAGFF QSDADEANIL RLHIPMKYGV YPMISGHKNR FAIKFMAFEN GQACSQDVEF
     ELAVCS