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Conserved domains on  [gi|15600245|ref|NP_253739|]
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hypothetical protein PA5052 [Pseudomonas aeruginosa PAO1]

Protein Classification

SPOR domain-containing protein( domain architecture ID 11459657)

SPOR domain-containing protein similar to Bacillus subtilis stage II sporulation protein B and Escherichia coli cell division proteins FtsN, DamX, and DedD

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
55-228 6.57e-19

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 81.21  E-value: 6.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245  55 RERPDAQRPAAVQGKQPQQNGQAQQPAQTQTPAQAKPKYEFYTLLPESEVVVPPEAVPEKAPPPPTPAELAKADEARAKA 134
Cdd:COG3087  25 AAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAAALAAASAAAAAAAAPAAAAAEAA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245 135 ALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVEAGNVRDETWYRVMVGPFNSRDQLSQAQKT 214
Cdd:COG3087 105 AAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLGLEARVVEVEVGGGTWYRVRVGPFSSRAEAEKAREK 184

                       170
                ....*....|....
gi 15600245 215 LSSNGFSNLLLQQR 228
Cdd:COG3087 185 LKAAGIDALVVRVK 198
 
Name Accession Description Interval E-value
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
55-228 6.57e-19

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 81.21  E-value: 6.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245  55 RERPDAQRPAAVQGKQPQQNGQAQQPAQTQTPAQAKPKYEFYTLLPESEVVVPPEAVPEKAPPPPTPAELAKADEARAKA 134
Cdd:COG3087  25 AAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAAALAAASAAAAAAAAPAAAAAEAA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245 135 ALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVEAGNVRDETWYRVMVGPFNSRDQLSQAQKT 214
Cdd:COG3087 105 AAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLGLEARVVEVEVGGGTWYRVRVGPFSSRAEAEKAREK 184

                       170
                ....*....|....
gi 15600245 215 LSSNGFSNLLLQQR 228
Cdd:COG3087 185 LKAAGIDALVVRVK 198
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 151-222 7.15e-11

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 56.60  E-value: 7.15e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600245   151 ASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVeAGNVRDETWYRVMVGPFNSRDQLSQAQKTLSSNGFSN 222
Cdd:pfam05036   1 ASGGYYVQLGAFSNEANAEALAAKLRAKGFAAYV-AVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLS 71
PRK12757 PRK12757
cell division protein FtsN; Provisional
 100-222 2.71e-08

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 52.74  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245  100 PESEVVVPPEAVPEKAPPPPTPAELAKADEARAKAALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLG 179
Cdd:PRK12757 130 PPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQRWMVQCGSFKGTEQAESVRAQLAFAG 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 15600245  180 QSVNVEAGNvrdeTWYRVMVGPFNSRDQLSQAQKTLSSNGFSN 222
Cdd:PRK12757 210 IESRITTGG----GWNRVVLGPYNSKAAADKMLQRLKGAGHSG 248
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 133-225 8.63e-07

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 48.53  E-value: 8.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245   133 KAALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVEAGNvrDETWYRVMVGPFNSRDQLSQAQ 212
Cdd:TIGR02223 206 TAPKADKADKTKPKPKEKAERAAALQCGAYANKEQAESVRAKLAFLGISSKITTTD--GGKWYRVVSGPYKNKDDAEKDL 283

                          90
                  ....*....|...
gi 15600245   213 KTLSSNGFSNLLL 225
Cdd:TIGR02223 284 NKLKVAGVAGCII 296
 
Name Accession Description Interval E-value
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
55-228 6.57e-19

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 81.21  E-value: 6.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245  55 RERPDAQRPAAVQGKQPQQNGQAQQPAQTQTPAQAKPKYEFYTLLPESEVVVPPEAVPEKAPPPPTPAELAKADEARAKA 134
Cdd:COG3087  25 AAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAAALAAASAAAAAAAAPAAAAAEAA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245 135 ALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVEAGNVRDETWYRVMVGPFNSRDQLSQAQKT 214
Cdd:COG3087 105 AAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLGLEARVVEVEVGGGTWYRVRVGPFSSRAEAEKAREK 184

                       170
                ....*....|....
gi 15600245 215 LSSNGFSNLLLQQR 228
Cdd:COG3087 185 LKAAGIDALVVRVK 198
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 100-215 2.77e-11

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 59.40  E-value: 2.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245 100 PESEVVVPPEAVPEKAPPPPTPAELAKADEARAKAALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLG 179
Cdd:COG3147  11 AAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAAAAPAAKAAAPAGGGWVVQLGAFSNEDNAKELVAKLRAAG 90

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600245 180 QSVNVEAGNVRDETWYRVMVGPFNSRDQLSQAQKTL 215
Cdd:COG3147  91 YPAYTEPVTTGGGTLYRVRVGPFASRAEAEAALAKL 126
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 151-222 7.15e-11

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 56.60  E-value: 7.15e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600245   151 ASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVeAGNVRDETWYRVMVGPFNSRDQLSQAQKTLSSNGFSN 222
Cdd:pfam05036   1 ASGGYYVQLGAFSNEANAEALAAKLRAKGFAAYV-AVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLS 71
PRK12757 PRK12757
cell division protein FtsN; Provisional
 100-222 2.71e-08

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 52.74  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245  100 PESEVVVPPEAVPEKAPPPPTPAELAKADEARAKAALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLG 179
Cdd:PRK12757 130 PPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQRWMVQCGSFKGTEQAESVRAQLAFAG 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 15600245  180 QSVNVEAGNvrdeTWYRVMVGPFNSRDQLSQAQKTLSSNGFSN 222
Cdd:PRK12757 210 IESRITTGG----GWNRVVLGPYNSKAAADKMLQRLKGAGHSG 248
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 133-225 8.63e-07

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 48.53  E-value: 8.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245   133 KAALAGQVPPPLPKAVVAASTQFFLQAGSFRKQSDADRVRAQIILLGQSVNVEAGNvrDETWYRVMVGPFNSRDQLSQAQ 212
Cdd:TIGR02223 206 TAPKADKADKTKPKPKEKAERAAALQCGAYANKEQAESVRAKLAFLGISSKITTTD--GGKWYRVVSGPYKNKDDAEKDL 283

                          90
                  ....*....|...
gi 15600245   213 KTLSSNGFSNLLL 225
Cdd:TIGR02223 284 NKLKVAGVAGCII 296
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
125-217 3.53e-05

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 43.90  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600245  125 AKADEARAKAALAGQVPPPLPKAVVAASTQFFLQAGSFrkqSDADRVRAQIILLGQSVNV-----EAGNVrdetwYRVMV 199
Cdd:PRK10672 260 TPTAPSSAPATAPAAAAPQAAATSSSASGNFVVQVGAV---SDQQRAQQWQQSLSQRFGVpgrvtQNGAV-----YRVQL 331

                         90
                 ....*....|....*...
gi 15600245  200 GPFNSRDQLSQAQKTLSS 217
Cdd:PRK10672 332 GPFASRQQASALQQRLQT 349
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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