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Conserved domains on  [gi|37288927|gb|AAQ90674|]
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cell division protein, partial [Bacillus sp. AH 1123]

Protein Classification

cell division protein FtsA( domain architecture ID 1000265)

cell division protein FtsA may serve as a membrane anchor for the Z ring; may be partial

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtsA super family cl34054
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
1-133 8.17e-51

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG0849:

Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 165.69  E-value: 8.17e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927   1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:COG0849  16 VVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGGHIKSQNSRGVVAI 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37288927  80 SneDREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:COG0849  96 S--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSG 147
 
Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
1-133 8.17e-51

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 165.69  E-value: 8.17e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927   1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:COG0849  16 VVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGGHIKSQNSRGVVAI 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37288927  80 SneDREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:COG0849  96 S--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSG 147
FtsA smart00842
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
1-133 7.44e-45

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.


Pssm-ID: 214850  Cd Length: 187  Bit Score: 144.54  E-value: 7.44e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927      1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:smart00842  11 IKALVAEVDEDgEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLKSVNVSGVVAI 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 37288927     80 snEDREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:smart00842  91 --PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSG 142
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
1-133 1.77e-40

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 138.05  E-value: 1.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927   1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:cd24048  13 ICALVGEVSEDgELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKHIRSVNSRGVIAI 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37288927  80 SNEDrEIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:cd24048  93 SDKD-EITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSG 145
ftsA TIGR01174
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
1-133 2.69e-39

cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]


Pssm-ID: 273483 [Multi-domain]  Cd Length: 371  Bit Score: 135.07  E-value: 2.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927     1 VKVIIGEMVNDS-LNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:TIGR01174  12 ICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHIKSQNSIGVVAI 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 37288927    80 SNEdrEIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:TIGR01174  92 KDK--EVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSG 143
ftsA PRK09472
cell division protein FtsA; Reviewed
1-133 5.82e-17

cell division protein FtsA; Reviewed


Pssm-ID: 181887 [Multi-domain]  Cd Length: 420  Bit Score: 75.59  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927    1 VKVIIGEMVNDS-LNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:PRK09472  20 VAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHISCQNEIGMVPI 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 37288927   80 SNEdrEIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:PRK09472 100 SEE--EVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSG 151
SHS2_FTSA pfam02491
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ...
73-133 1.56e-16

SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. The SHS2 domain is inserted in to the RNAseH fold of FtsA, and is involved in protein-protein interaction.


Pssm-ID: 460571 [Multi-domain]  Cd Length: 73  Bit Score: 68.67  E-value: 1.56e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37288927    73 CHGVVAVSNedREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:pfam02491   4 SSGVVAISG--REITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSG 62
 
Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
1-133 8.17e-51

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 165.69  E-value: 8.17e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927   1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:COG0849  16 VVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGGHIKSQNSRGVVAI 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37288927  80 SneDREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:COG0849  96 S--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSG 147
FtsA smart00842
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
1-133 7.44e-45

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.


Pssm-ID: 214850  Cd Length: 187  Bit Score: 144.54  E-value: 7.44e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927      1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:smart00842  11 IKALVAEVDEDgEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLKSVNVSGVVAI 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 37288927     80 snEDREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:smart00842  91 --PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSG 142
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
1-133 1.77e-40

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 138.05  E-value: 1.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927   1 VKVIIGEMVND-SLNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:cd24048  13 ICALVGEVSEDgELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKHIRSVNSRGVIAI 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37288927  80 SNEDrEIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:cd24048  93 SDKD-EITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSG 145
ftsA TIGR01174
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
1-133 2.69e-39

cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]


Pssm-ID: 273483 [Multi-domain]  Cd Length: 371  Bit Score: 135.07  E-value: 2.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927     1 VKVIIGEMVNDS-LNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:TIGR01174  12 ICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHIKSQNSIGVVAI 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 37288927    80 SNEdrEIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:TIGR01174  92 KDK--EVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSG 143
ftsA PRK09472
cell division protein FtsA; Reviewed
1-133 5.82e-17

cell division protein FtsA; Reviewed


Pssm-ID: 181887 [Multi-domain]  Cd Length: 420  Bit Score: 75.59  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37288927    1 VKVIIGEMVNDS-LNIIGVGNVKSNGLKKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGVNANQVQLLPCHGVVAV 79
Cdd:PRK09472  20 VAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHISCQNEIGMVPI 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 37288927   80 SNEdrEIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:PRK09472 100 SEE--EVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSG 151
SHS2_FTSA pfam02491
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ...
73-133 1.56e-16

SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. The SHS2 domain is inserted in to the RNAseH fold of FtsA, and is involved in protein-protein interaction.


Pssm-ID: 460571 [Multi-domain]  Cd Length: 73  Bit Score: 68.67  E-value: 1.56e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37288927    73 CHGVVAVSNedREIGNEDVLRVLDAAQVVSIAPEREFIDVVPRQFIVDGLDEINDPRGMIG 133
Cdd:pfam02491   4 SSGVVAISG--REITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSG 62
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
1-63 1.44e-06

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 45.75  E-value: 1.44e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37288927   1 VKVIIGEMVNDSLNIIGVGNVKSNGL--KKGSIVDIDETVRSIKKAIEQAERMVGIHIEQVVVGV 63
Cdd:cd24004  10 IKGLVLEEDDENIEVLAFSSEEHPERamGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAI 74
 
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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