ID   POMZ_MYXXD              Reviewed;         319 AA.
AC   Q1DEM0; Q84FD9;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cell division protein PomZ {ECO:0000305};
DE   AltName: Full=Adventurous gliding motility protein E {ECO:0000303|PubMed:12828649};
DE   AltName: Full=Positioning at midcell of FtsZ {ECO:0000303|PubMed:23145985};
GN   Name=pomZ {ECO:0000303|PubMed:23145985};
GN   Synonyms=agmE {ECO:0000303|PubMed:12828649};
GN   OrderedLocusNames=MXAN_0635 {ECO:0000312|EMBL:ABF86116.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=DK1622;
RX   PubMed=12828649; DOI=10.1046/j.1365-2958.2003.03582.x;
RA   Youderian P.A., Burke N., White D.J., Hartzell P.L.;
RT   "Identification of genes required for adventurous gliding motility in
RT   Myxococcus xanthus with the transposable element mariner.";
RL   Mol. Microbiol. 49:555-570(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN   [3]
RP   FUNCTION, POSSIBLE INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF ASP-90.
RC   STRAIN=DK1622;
RX   PubMed=23145985; DOI=10.1111/mmi.12094;
RA   Treuner-Lange A., Aguiluz K., van der Does C., Gomez-Santos N., Harms A.,
RA   Schumacher D., Lenz P., Hoppert M., Kahnt J., Munoz-Dorado J.,
RA   Soegaard-Andersen L.;
RT   "PomZ, a ParA-like protein, regulates Z-ring formation and cell division in
RT   Myxococcus xanthus.";
RL   Mol. Microbiol. 87:235-253(2013).
CC   -!- FUNCTION: Spatial regulator of cell division that is involved in
CC       identifying the incipient division site, recruiting FtsZ to the
CC       division site and stabilizing the Z-ring. Binds ATP and GTP.
CC       {ECO:0000269|PubMed:23145985}.
CC   -!- SUBUNIT: Interacts with FtsZ in pull-down experiments.
CC       {ECO:0000269|PubMed:23145985}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Localization is
CC       dynamic and cell cycle regulated. Accumulates at the division site at
CC       mid-cell after chromosome segregation but prior to FtsZ as well as in
CC       the absence of FtsZ. {ECO:0000269|PubMed:23145985}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in division defects with the
CC       formation of filamentous cells and chromosome-free minicells. It causes
CC       reduced formation of Z-rings and incorrect positioning of the few Z-
CC       rings formed. Deletion does not affect chromosome replication and
CC       segregation (PubMed:23145985). Inactivation affects adventurous (A)
CC       gliding motility (PubMed:12828649). {ECO:0000269|PubMed:12828649,
CC       ECO:0000269|PubMed:23145985}.
CC   -!- SIMILARITY: Belongs to the ParA family. {ECO:0000305}.
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DR   EMBL; AY204464; AAO22874.1; -; Genomic_DNA.
DR   EMBL; CP000113; ABF86116.1; -; Genomic_DNA.
DR   RefSeq; WP_011550766.1; NC_008095.1.
DR   AlphaFoldDB; Q1DEM0; -.
DR   SMR; Q1DEM0; -.
DR   STRING; 246197.MXAN_0635; -.
DR   EnsemblBacteria; ABF86116; ABF86116; MXAN_0635.
DR   GeneID; 41358113; -.
DR   KEGG; mxa:MXAN_0635; -.
DR   eggNOG; COG1192; Bacteria.
DR   HOGENOM; CLU_037612_1_2_7; -.
DR   OMA; RVWAVAN; -.
DR   OrthoDB; 729012at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13614; AAA_31; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cytoplasm; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..319
FT                   /note="Cell division protein PomZ"
FT                   /id="PRO_0000436617"
FT   BINDING         61..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
FT   MUTAGEN         90
FT                   /note="D->A: Lack of activity. Cannot complement the
FT                   deletion mutant."
FT                   /evidence="ECO:0000269|PubMed:23145985"
SQ   SEQUENCE   319 AA;  35218 MW;  A6149C23EC3DAB02 CRC64;
     MEAPTYSSKQ VAEMLGVSPK QIPEESRKDA YTPDDIWELR TTLDRFPARL GHRRQLFLNF
     KGGTGKTSLS TSYAWRLAEL GYAVLLIDLD SQGHATKCLG YEGEDFEKTL LDVLVRKTPL
     AKVIQKSSLP NLDFVPSNLT MSTVDLALMP MAGREFKLRN ALKDVEAQYD VVVFDAPPSF
     GLLNLNALMA ANDLFVPVLA DFLSFHGLKL LFETVQSLEE DLNHVLDHVF IVVNSFNATF
     KLAKEALEAL QTHYPEFLLP TIIRQCTKFA QASSEGRPVF VADPSSKGAN DIQAMIDNIL
     PRLVAAAAVA QTKGTQQAG