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. 2010 Jun;74(2):273–297. doi: 10.1128/MMBR.00048-09

TABLE 2.

Conservation of cell division proteins in Acinetobacter spp.

Protein Function Protein locationa Protein length (amino acids)b % Sequence identity (residue range)
Essentialitye Homologs with known structuresb (residue range of sequence match; % sequence identity) Known protein-protein interactions in E. coli Reference(s)
A. baylyi vs E. colic A. baumannii vs E. colid A. baylyi vs A. baumanniic
FtsA Tethers FtsZ to membrane, stabilizes Z rings at membrane c 420 29 (8-409) 30 (8-409) 88 (1-420) A, E, P Thermotoga maritima (10-351; 23) FtsZ 101, 207, 249, 257
FtsB (DivIC) Unknown; role in septal peptidoglycan synthesis? m 110 41 (6-77) 38 (25-96) 91 (6-110) A, E, P f FtsQ, FtsL 28, 92
FtsE Unknown; similar to ABC transporter c E FtsZ, FtsX 46, 218, 227
FtsI/PBP3 (PBPB) Cross-links septal peptidoglycan m 621 40 (15-607) 39 (7-598) 89 (10-617) A, E, P FtsQ, FtsN 66, 69
FtsK Role in chromosome segregation and septum formation m 1018 60 (528-1017) 59 (516-1009) 77 (1-1018) A, E, P Pseudomonas aeruginosa (527-942; 59), E. coli (528-1017; 59) FtsZ, FtsL, FtsQ 66, 169
FtsL Unknown; role in septal peptidoglycan synthesis? m 110 24 (26-100) 26 (28-100) 88 (29-109) A, E, P FtsQ, FtsB, FtsW, FtsK 28, 66, 69
FtsN Unknown m 200 23 (44-197) 16 (3-206) 87 (1-200) A, E, P E. coli (120-200; 19) FtsQ, FtsI, FtsW 52, 53, 66, 69, 268
FtsQ (DivIB) Unknown; role in septal peptidoglycan synthesis? m 284 25 (61-261) 26 (90-259) 81 (1-284) A, E, P Yersinia enterocolitica (59-266; 24), E. coli (61-267; 23) FtsB, FtsL, FtsI, FtsN, FtsW, FtsK 28, 34, 69, 220, 250
FtsW Septal peptidoglycan synthesis m 399 42 (32-388) 42 (31-387) 85 (2-399) A, E, P FtsI, FtsL, FtsN, FtsQ 66, 69
FtsX Unknown; similar to ABC transporter m E FtsE 218, 227
FtsZ First protein to form midcell ring in cell division c 389 47 (31-386) 48 (31-388) 90 (1-389) A, E, P P. aeruginosa (31-322; 55), B. subtilis (35-389; 46), Mycobacterium tuberculosis (31-322; 53), Methanococcus jannaschii (5-322; 42), A. aeolicus (31-320; 43) FtsA, ZapA, ZapB, ZipA, FtsE, FtsK, MinC, SulA, ClpX, SlmA 22, 46, 66, 71, 79, 95, 98, 101, 108, 110, 151, 160, 161, 165, 179, 193, 194, 207, 228, 257
ZapA Promotes FtsZ polymerization and protofilament bundling c 94 21 (7-94) 26 (1-88) 80 (1-92) D Pseudomonas aeruginosa (1-93; 16) FtsZ 95, 160
ZapB Promotes FtsZ polymerization c D FtsZ 71
ZipA Stabilizes Z rings at membrane m 325 28 (185-310) 27 (205-330) 62 (1-324) E E. coli (183-323; 26) FtsZ 98, 101, 179
MinC cell division inhibitor c 240 40 (111-230) 41 (122-229) 78 (1-240) D T. maritima (111-213; 28) MinD, FtsZ 47, 108-110, 193, 228
MinD Membrane ATPase of the MinC-MinD-MinE system m 278 64 (9-278) 65 (9-278) 95 (1-278) E Archaeglobus fulgidis (9-277; 30), Pyrococcus furiosus (9-256; 30) MinC, MinE 48, 104, 108-110, 224
MinE Cell division topological specificity factor c 90 33 (9-88) 32 (9-88) 92 (1-90) E E. coli (36-90; 28) MinD 62, 110, 147, 214, 278
SlmA Spatial regulation of Z-ring formation (nucleoid occlusion) c D FtsZ 22
SulA FtsZ assembly inhibitor c D P. aeruginosa (no homolog) FtsZ 49, 110
ClpX FtsZ assembly inhibitor m 436 70 (10-408) 71 (10-408) 91 (1-436) D Helicobacter pylori (54-417; 58) FtsZ 32, 79, 146
AmiC Amidase; required for septal wall degradation and cell separation p D 20
EnvC Murein hydrolase; required for septal wall degradation and cell separation p D 21
a

c, cytoplasmic; p, periplasmic; m, membrane associated.

b

Acinetobacter baylyi protein (15).

c

Determined from BLAST output (6); residue range is for A. baylyi protein (15).

d

Determined from BLAST output (6); residue range is for A. baumannii AYE protein (248).

e

A, essential in Acinetobacter baylyi (61); P, essential in Pseudomonas aeruginosa (118); E, essential in Escherichia coli (11); D, dispensable gene.

f

—, not applicable, no structure determined, or not present in Acinetobacter spp.