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Conserved domains on  [gi|499405421|ref|WP_011092888|]
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endolytic peptidoglycan transglycosylase RlpA [Pectobacterium atrosepticum]

Protein Classification

septal ring lytic transglycosylase RlpA family protein( domain architecture ID 11484865)

septal ring lytic transglycosylase RlpA family protein similar to endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
1-368 0e+00

endolytic peptidoglycan transglycosylase RlpA;


:

Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 587.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   1 MRKDWLWVGVATLALAACTTTEQRQ--PAPPVTQVYSGPTEEIGGAEPRYEPYNQGTLQDYSIKGKTYKIVKNPQNFSEA 78
Cdd:PRK10672   1 MRKQWLGIGIAAGLLAACTSDDGQQqtVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKIVQDPSNFSQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  79 GLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNISN 158
Cdd:PRK10672  81 GLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 159 NTKVKVDFINVAPDGTLSGPGTAGTTVAKQSFSLPERPSFgASGLGTPMMETTsPTSNSAVRPISNSGLNTpaenaQPQS 238
Cdd:PRK10672 161 NTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDL-SGGMGTPSVQPA-PAPQGDVLPVSNSTLKS-----EDPT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 239 STPSHGGGFLGAPSALRAGVVEPNMTPTTTPSTAPmnVAPVAAAVTAPVATTPSATGRYVVQVGALSDQQRAQTWQRSLS 318
Cdd:PRK10672 234 GAPVTSSGFLGAPTTLAPGVLEGSEPTPTAPSSAP--ATAPAAAAPQAAATSSSASGNFVVQVGAVSDQQRAQQWQQSLS 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 499405421 319 ERFRVAGKVTASGGLYRIQLGPFQNRQQAAELQQRLSVEAQQQSFITAAP 368
Cdd:PRK10672 312 QRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFITTAQ 361
 
Name Accession Description Interval E-value
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
1-368 0e+00

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 587.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   1 MRKDWLWVGVATLALAACTTTEQRQ--PAPPVTQVYSGPTEEIGGAEPRYEPYNQGTLQDYSIKGKTYKIVKNPQNFSEA 78
Cdd:PRK10672   1 MRKQWLGIGIAAGLLAACTSDDGQQqtVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKIVQDPSNFSQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  79 GLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNISN 158
Cdd:PRK10672  81 GLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 159 NTKVKVDFINVAPDGTLSGPGTAGTTVAKQSFSLPERPSFgASGLGTPMMETTsPTSNSAVRPISNSGLNTpaenaQPQS 238
Cdd:PRK10672 161 NTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDL-SGGMGTPSVQPA-PAPQGDVLPVSNSTLKS-----EDPT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 239 STPSHGGGFLGAPSALRAGVVEPNMTPTTTPSTAPmnVAPVAAAVTAPVATTPSATGRYVVQVGALSDQQRAQTWQRSLS 318
Cdd:PRK10672 234 GAPVTSSGFLGAPTTLAPGVLEGSEPTPTAPSSAP--ATAPAAAAPQAAATSSSASGNFVVQVGAVSDQQRAQQWQQSLS 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 499405421 319 ERFRVAGKVTASGGLYRIQLGPFQNRQQAAELQQRLSVEAQQQSFITAAP 368
Cdd:PRK10672 312 QRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFITTAQ 361
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 54-174 5.09e-59

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 187.37  E-value: 5.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  54 GTLQDYSIKGKTYKIVKNPQNFSEAGLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVN 133
Cdd:COG0797   11 ASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRVN 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499405421 134 DRGPYTPGRIIDLSKAAGDRLNISNNTKVKVDFINVAPDGT 174
Cdd:COG0797   91 DRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASL 131
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 77-165 7.62e-43

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 144.13  E-value: 7.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  77 EAGLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNI 156
Cdd:cd22268    1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGM 80

                         90
                 ....*....|.
gi 499405421 157 --SNNTKVKVD 165
Cdd:cd22268   81 lgAGVAPVRIE 91
rlpA TIGR00413
rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. ...
 79-193 1.70e-32

rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA. [Cell envelope, Other]


Pssm-ID: 273065 [Multi-domain]  Cd Length: 208  Bit Score: 120.86  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   79 GLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNI-- 156
Cdd:TIGR00413   1 GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSHAAAREIGLis 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499405421  157 SNNTKVKVDFINVAPDGTLSGPgtagttvAKQSFSLP 193
Cdd:TIGR00413  81 RGVGQVRIEVLHVAKNGNLSGA-------ATKTFNKQ 110
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 77-166 5.41e-27

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 102.28  E-value: 5.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   77 EAGLATWYGeeasgNRTSIGEVFDPNAITAAHPTLPLPSYVRVtnlSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNI 156
Cdd:pfam03330   1 AAGSASLYN-----NGTACGECYDVRCLTAAHPTLPFGTYCRV---LSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72

                          90
                  ....*....|
gi 499405421  157 SNNTKVKVDF 166
Cdd:pfam03330  73 PRAGIVPVQY 82
 
Name Accession Description Interval E-value
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
1-368 0e+00

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 587.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   1 MRKDWLWVGVATLALAACTTTEQRQ--PAPPVTQVYSGPTEEIGGAEPRYEPYNQGTLQDYSIKGKTYKIVKNPQNFSEA 78
Cdd:PRK10672   1 MRKQWLGIGIAAGLLAACTSDDGQQqtVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKIVQDPSNFSQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  79 GLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNISN 158
Cdd:PRK10672  81 GLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 159 NTKVKVDFINVAPDGTLSGPGTAGTTVAKQSFSLPERPSFgASGLGTPMMETTsPTSNSAVRPISNSGLNTpaenaQPQS 238
Cdd:PRK10672 161 NTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDL-SGGMGTPSVQPA-PAPQGDVLPVSNSTLKS-----EDPT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 239 STPSHGGGFLGAPSALRAGVVEPNMTPTTTPSTAPmnVAPVAAAVTAPVATTPSATGRYVVQVGALSDQQRAQTWQRSLS 318
Cdd:PRK10672 234 GAPVTSSGFLGAPTTLAPGVLEGSEPTPTAPSSAP--ATAPAAAAPQAAATSSSASGNFVVQVGAVSDQQRAQQWQQSLS 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 499405421 319 ERFRVAGKVTASGGLYRIQLGPFQNRQQAAELQQRLSVEAQQQSFITAAP 368
Cdd:PRK10672 312 QRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFITTAQ 361
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 54-174 5.09e-59

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 187.37  E-value: 5.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  54 GTLQDYSIKGKTYKIVKNPQNFSEAGLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVN 133
Cdd:COG0797   11 ASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRVN 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499405421 134 DRGPYTPGRIIDLSKAAGDRLNISNNTKVKVDFINVAPDGT 174
Cdd:COG0797   91 DRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASL 131
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 77-165 7.62e-43

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 144.13  E-value: 7.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421  77 EAGLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNI 156
Cdd:cd22268    1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGM 80

                         90
                 ....*....|.
gi 499405421 157 --SNNTKVKVD 165
Cdd:cd22268   81 lgAGVAPVRIE 91
rlpA TIGR00413
rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. ...
 79-193 1.70e-32

rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA. [Cell envelope, Other]


Pssm-ID: 273065 [Multi-domain]  Cd Length: 208  Bit Score: 120.86  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   79 GLATWYGEEASGNRTSIGEVFDPNAITAAHPTLPLPSYVRVTNLSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNI-- 156
Cdd:TIGR00413   1 GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSHAAAREIGLis 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499405421  157 SNNTKVKVDFINVAPDGTLSGPgtagttvAKQSFSLP 193
Cdd:TIGR00413  81 RGVGQVRIEVLHVAKNGNLSGA-------ATKTFNKQ 110
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 77-166 5.41e-27

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 102.28  E-value: 5.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421   77 EAGLATWYGeeasgNRTSIGEVFDPNAITAAHPTLPLPSYVRVtnlSNGRRLVVRVNDRGPYTPGRIIDLSKAAGDRLNI 156
Cdd:pfam03330   1 AAGSASLYN-----NGTACGECYDVRCLTAAHPTLPFGTYCRV---LSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72

                          90
                  ....*....|
gi 499405421  157 SNNTKVKVDF 166
Cdd:pfam03330  73 PRAGIVPVQY 82
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 293-364 7.08e-13

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: 63.53  E-value: 7.08e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499405421  293 ATGRYVVQVGALSDQQRAQTWQRSLSERFRVAG--KVTASGGLYRIQLGPFQNRQQAAELQQRLSVEAQQQSFI 364
Cdd:pfam05036   1 ASGGYYVQLGAFSNEANAEALAAKLRAKGFAAYvaVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPFV 74
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 292-368 1.49e-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: 61.71  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499405421 292 SATGRYVVQVGALSDQQRAQTWQRSLSER-FRV-AGKVTASGG-LYRIQLGPFQNRQQAAELQQRLSVEAQQQSFITAAP 368
Cdd:COG3147   61 PAGGGWVVQLGAFSNEDNAKELVAKLRAAgYPAyTEPVTTGGGtLYRVRVGPFASRAEAEAALAKLKKLTGLKGFVVRYK 140
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
297-367 1.11e-08

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


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 54.63  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499405421 297 YVVQVGALSDQQRAQTWQRSLSERF---RVAGKVTASGGLYRIQLGPFQNRQQAAELQQRLSVEAQQQSFITAA 367
Cdd:COG3087  125 YYVQVGAFRSRANAERLRARLALLGleaRVVEVEVGGGTWYRVRVGPFSSRAEAEKAREKLKAAGIDALVVRVK 198
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 296-357 1.95e-04

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: 42.76  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499405421  296 RYVVQVGALSDQQRAQTWQRSLSerfrVAG---KVTASGG--LYRIQLGPFQNRQQAAELQQRLSVE 357
Cdd:TIGR02223 227 AAALQCGAYANKEQAESVRAKLA----FLGissKITTTDGgkWYRVVSGPYKNKDDAEKDLNKLKVA 289
 
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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