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Is a key regulator of cell envelope growth, playing a crucial role in coordinating cell width, elongation and division to maintain cell envelope integrity (PubMed:34941903). Plays an important role in the lipopolysaccharide (LPS) assembly/transport (PubMed:36077106). It may regulate LpxC levels and assist MsbA-mediated LPS transport (PubMed:36077106)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21210718"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27335665"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33895137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36077106"}],"value":"Forms homooligomers (PubMed:21210718). Interacts with proteins of the divisome, such as FtsI and FtsQ, and of the elongasome, such as RodZ and RodA (PubMed:27335665, PubMed:33895137). Also interacts several other proteins, including the shape-determining proteins MreC and MreD, the N-acetylglucosaminyl transferase MurG and the lipopolysaccharide assembly protein LapA (PubMed:27335665). It also copurifies with LapB and various proteins involved in LPS biosynthesis/transport and phospholipid biosynthesis (PubMed:36077106)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16079137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21210718"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16079137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21210718"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16863643"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27335665"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32323199"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33895137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34941903"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36077106"}],"value":"Deletion of the gene results in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth, defects in DNA segregation and generation of chromosome-less cells (PubMed:32323199, PubMed:33895137). It also shows abnormal FtsZ ring formation and aberrant septum development (PubMed:33895137). Deletion causes high sensitivities to various envelope stresses, loss of envelope stability, increased membrane permeability and causes growth defect under normal growth conditions (PubMed:32323199, PubMed:34941903). Loss of the gene results in aberrant cell size driven by the production of excess membrane phospholipids (PubMed:34941903). The knockout mutant does not grow at 45 degrees Celsius and is hypersensitive to cell wall-acting antibiotics, even in the stationary phase (PubMed:33895137). Mutant is highly susceptible to vancomycin and various anti-folate antibiotics such as such as trimethoprim, sulfanilamide and sulfamethazine (PubMed:32323199). Loss of the gene causes a reduction in LpxC amounts and LPS defects (PubMed:36077106). The deletion of both zapG and rodZ genes causes synthetic lethality (PubMed:27335665, PubMed:34941903). Deletion is also synthetically lethal with components of peptidoglycan synthesis and recycling pathways (PubMed:34941903). No change in function or assembly of the cytochrome bd-I complex (PubMed:16863643)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ZapG family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16079137"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16863643"}],"value":"Was originally thought to be a member of the cytochrome bd-I complex (PubMed:16079137). Subsequent work suggests this is not the case (PubMed:16863643)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAA58035.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Z-ring associated protein G","featureId":"PRO_0000169477"},{"type":"Transmembrane","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21210718"}]},{"type":"Region","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"id":"KW-0132","category":"Biological process","name":"Cell division"},{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. 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