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Conserved domains on  [gi|446264327|ref|WP_000342182|]
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MULTISPECIES: cell division protein FtsQ/DivIB [Staphylococcus]

Protein Classification

cell division protein FtsQ/DivIB( domain architecture ID 11446343)

cell division protein FtsQ/DivIB may be involved in stabilizing or promoting the assembly of the division complex

CATH:  3.40.50.10960
Gene Ontology:  GO:0051301|GO:0043093
SCOP:  4004200

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtsQ COG1589
Cell division septal protein FtsQ [Cell cycle control, cell division, chromosome partitioning]; ...
175-394 3.02e-46

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


:

Pssm-ID: 441197 [Multi-domain]  Cd Length: 241  Bit Score: 159.81  E-value: 3.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 175 VITILVLLIAVILIYMFSPLSKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLPN 254
Cdd:COG1589   20 LLLLLLLLALLVWLLLFSPLFPVREVEVEGNSHVSAEEIRAALGILLGGNLFTLDLDAIRERLEALPWVKSASVRRRWPD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 255 TLNVDITENEIIALVKYKGKYLPLLENGKLLKGSNDVKINDAPVMDGFKGTKED--DMIKALSEMtPEVRRYIAEVTYap 332
Cdd:COG1589  100 TLVIEVTEREPVARWNTGGGYYLVDADGVVFEAVSAEPPADLPLLTGPDGSEKAvlALLELLAAL-PELRLQISEISL-- 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446264327 333 skNKQSRIELFTTDGLQVI-GDISTISKKMKYYPQMSQSLSRDSSGKlktrgYIDLSVGASFI 394
Cdd:COG1589  177 --SSRGRWTLTLDDGVEVRlGRSEDLAEKLARLAALLPQLLAGKGIA-----YIDLRYPDGPA 232
 
Name Accession Description Interval E-value
FtsQ COG1589
Cell division septal protein FtsQ [Cell cycle control, cell division, chromosome partitioning]; ...
175-394 3.02e-46

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


Pssm-ID: 441197 [Multi-domain]  Cd Length: 241  Bit Score: 159.81  E-value: 3.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 175 VITILVLLIAVILIYMFSPLSKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLPN 254
Cdd:COG1589   20 LLLLLLLLALLVWLLLFSPLFPVREVEVEGNSHVSAEEIRAALGILLGGNLFTLDLDAIRERLEALPWVKSASVRRRWPD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 255 TLNVDITENEIIALVKYKGKYLPLLENGKLLKGSNDVKINDAPVMDGFKGTKED--DMIKALSEMtPEVRRYIAEVTYap 332
Cdd:COG1589  100 TLVIEVTEREPVARWNTGGGYYLVDADGVVFEAVSAEPPADLPLLTGPDGSEKAvlALLELLAAL-PELRLQISEISL-- 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446264327 333 skNKQSRIELFTTDGLQVI-GDISTISKKMKYYPQMSQSLSRDSSGKlktrgYIDLSVGASFI 394
Cdd:COG1589  177 --SSRGRWTLTLDDGVEVRlGRSEDLAEKLARLAALLPQLLAGKGIA-----YIDLRYPDGPA 232
POTRA_1 pfam08478
POTRA domain, FtsQ-type; FtsQ/DivIB bacterial division proteins (pfam03799) contain an ...
195-262 3.05e-17

POTRA domain, FtsQ-type; FtsQ/DivIB bacterial division proteins (pfam03799) contain an N-terminal POTRA domain (for polypeptide-transport-associated domain). This is found in different types of proteins, usually associated with a transmembrane beta-barrel. FtsQ/DivIB may have chaperone-like roles, which has also been postulated for the POTRA domain in other contexts.


Pssm-ID: 430019 [Multi-domain]  Cd Length: 69  Bit Score: 75.68  E-value: 3.05e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446264327  195 SKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLPNTLNVDITE 262
Cdd:pfam08478   1 FPIRQVEVSGNKHLSTEEIRKALGIQLGTSFFSLDLNAIEDRLEKLPWVKSATVRRQWPNTLRITVTE 68
PRK05529 PRK05529
cell division protein FtsQ; Provisional
174-270 1.13e-03

cell division protein FtsQ; Provisional


Pssm-ID: 135428 [Multi-domain]  Cd Length: 255  Bit Score: 40.67  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 174 SVITILVLLIAVILIyMFSPLSKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLP 253
Cdd:PRK05529  41 AVGAVLTLLLFVMLS-AYSPLLALRSIEVAGNMRVKPQDIVAALRDQFGKPLPLVDPETVRKKLAAFPLIRSYSVESKPP 119
                         90
                 ....*....|....*..
gi 446264327 254 NTLNVDITENEIIALVK 270
Cdd:PRK05529 120 GTIVVRVVERVPLAFIQ 136
 
Name Accession Description Interval E-value
FtsQ COG1589
Cell division septal protein FtsQ [Cell cycle control, cell division, chromosome partitioning]; ...
175-394 3.02e-46

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


Pssm-ID: 441197 [Multi-domain]  Cd Length: 241  Bit Score: 159.81  E-value: 3.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 175 VITILVLLIAVILIYMFSPLSKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLPN 254
Cdd:COG1589   20 LLLLLLLLALLVWLLLFSPLFPVREVEVEGNSHVSAEEIRAALGILLGGNLFTLDLDAIRERLEALPWVKSASVRRRWPD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 255 TLNVDITENEIIALVKYKGKYLPLLENGKLLKGSNDVKINDAPVMDGFKGTKED--DMIKALSEMtPEVRRYIAEVTYap 332
Cdd:COG1589  100 TLVIEVTEREPVARWNTGGGYYLVDADGVVFEAVSAEPPADLPLLTGPDGSEKAvlALLELLAAL-PELRLQISEISL-- 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446264327 333 skNKQSRIELFTTDGLQVI-GDISTISKKMKYYPQMSQSLSRDSSGKlktrgYIDLSVGASFI 394
Cdd:COG1589  177 --SSRGRWTLTLDDGVEVRlGRSEDLAEKLARLAALLPQLLAGKGIA-----YIDLRYPDGPA 232
POTRA_1 pfam08478
POTRA domain, FtsQ-type; FtsQ/DivIB bacterial division proteins (pfam03799) contain an ...
195-262 3.05e-17

POTRA domain, FtsQ-type; FtsQ/DivIB bacterial division proteins (pfam03799) contain an N-terminal POTRA domain (for polypeptide-transport-associated domain). This is found in different types of proteins, usually associated with a transmembrane beta-barrel. FtsQ/DivIB may have chaperone-like roles, which has also been postulated for the POTRA domain in other contexts.


Pssm-ID: 430019 [Multi-domain]  Cd Length: 69  Bit Score: 75.68  E-value: 3.05e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446264327  195 SKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLPNTLNVDITE 262
Cdd:pfam08478   1 FPIRQVEVSGNKHLSTEEIRKALGIQLGTSFFSLDLNAIEDRLEKLPWVKSATVRRQWPNTLRITVTE 68
FtsQ_DivIB_C pfam03799
Cell division protein FtsQ/DivIB, C-terminal; FtsQ is an essential cell division protein. It ...
267-387 1.93e-11

Cell division protein FtsQ/DivIB, C-terminal; FtsQ is an essential cell division protein. It may link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. FtsQ may control the correct divisome assembly. DivIB is a cell division protein from Gram-positive bacteria, probably homologous to Escherichia coli FtsQ. DivIB interacts with FtsL, DivIC and PBP-2B. DivIB plays an essential role in division at high temperatures, maybe by protecting FtsL from degradation or by promoting formation of the FtsL-DivIC complex. It is also required for efficient sporulation at all temperatures. FtsQ and DivIB have a short N-terminal cytoplasmic domain and a larger C-terminal periplasmic domain. This entry represents the C-terminal region.


Pssm-ID: 461056  Cd Length: 113  Bit Score: 60.89  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327  267 ALVKYKGKYLPLLENGKLLKGSNDVKinDAPVMDGFKGtKEDDMIKALSEMTPEVRRYIAEVTyapsKNKQSRIELFTTD 346
Cdd:pfam03799   1 ARWQQGGYLYLVDADGEVFEAFADNA--GLPVLTGPEG-SAKEVLALLAALPPELKPRISEIS----LSARRRWTLMLDD 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446264327  347 GLQVI---GDISTISKKMKYYPQMSQSLSRdssgKLKTRGYIDL 387
Cdd:pfam03799  74 GIEVRlgrEDVEEDLAKLQRFVQLYPQLEE----LGRDIEYIDL 113
PRK05529 PRK05529
cell division protein FtsQ; Provisional
174-270 1.13e-03

cell division protein FtsQ; Provisional


Pssm-ID: 135428 [Multi-domain]  Cd Length: 255  Bit Score: 40.67  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 174 SVITILVLLIAVILIyMFSPLSKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQLP 253
Cdd:PRK05529  41 AVGAVLTLLLFVMLS-AYSPLLALRSIEVAGNMRVKPQDIVAALRDQFGKPLPLVDPETVRKKLAAFPLIRSYSVESKPP 119
                         90
                 ....*....|....*..
gi 446264327 254 NTLNVDITENEIIALVK 270
Cdd:PRK05529 120 GTIVVRVVERVPLAFIQ 136
BamA COG4775
Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis];
197-336 6.76e-03

Outer membrane protein assembly factor BamA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443807 [Multi-domain]  Cd Length: 711  Bit Score: 38.92  E-value: 6.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446264327 197 IAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEEDPLIKSVEIHKQlPNTLNVDITENEIIALVKYKGkyl 276
Cdd:COG4775    1 IKDIRVEGLQRVEAGTVLSYLPLRVGDTFDDEKLDEAIKALYATGLFSDVRIERE-GVVLVVKVKERPTINSIEFEG--- 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446264327 277 plleNGKL----LKGSNDVKINDApvmdgFKGTKEDDMIKALSEMTPEVRRYIAEVTYAPSKNK 336
Cdd:COG4775   77 ----NKKIkdedLKKELGLKEGRV-----FDRALLERAEQELKEQYRSKGYYNAKVTITPERNR 131
 
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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