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Conserved domains on  [gi|489736755|ref|WP_003640850|]
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MULTISPECIES: DivIVA domain-containing protein [Lactiplantibacillus]

Protein Classification

DivIVA domain-containing protein( domain architecture ID 12060610)

DivIVA domain-containing protein similar to Bacillus subtilis septum site-determining protein DivIVA, which may act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 3-144 8.45e-47

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


:

Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 151.18  E-value: 8.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755    3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQERLDSSEGKLKYFNELKDSLNQSILVAQEAADKVK 82
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489736755   83 TNSKKEADIITREAQKQAsdivseatdksNQMIDEASQKAKRLSVETDDLKKQTRVFRQRLQ 144
Cdd:pfam05103  81 ANAQKEAELIIKEAEAKA-----------ERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
 
Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 3-144 8.45e-47

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 151.18  E-value: 8.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755    3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQERLDSSEGKLKYFNELKDSLNQSILVAQEAADKVK 82
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489736755   83 TNSKKEADIITREAQKQAsdivseatdksNQMIDEASQKAKRLSVETDDLKKQTRVFRQRLQ 144
Cdd:pfam05103  81 ANAQKEAELIIKEAEAKA-----------ERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1-136 1.21e-41

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 138.06  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755   1 MVLSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQERLDSSEGKLKYFNELKDSLNQSILVAQEAADK 80
Cdd:COG3599    1 MKLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489736755  81 VKTNSKKEADIITREAQKQASDIVSEATDKSNQMIDeasqkakrlsvETDDLKKQT 136
Cdd:COG3599   81 VKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVR-----------EIEELKRQR 125
DivI1A_domain TIGR03544
DivIVA domain; This model describes a domain found in Bacillus subtilis cell division ...
 3-36 2.31e-12

DivIVA domain; This model describes a domain found in Bacillus subtilis cell division initiation protein DivIVA, and homologs, toward the N-terminus. It is also found as a repeated domain in certain other proteins, including family TIGR03543.


Pssm-ID: 274639 [Multi-domain]  Cd Length: 34  Bit Score: 59.36  E-value: 2.31e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489736755    3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDY 36
Cdd:TIGR03544   1 LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL 34
PRK14127 PRK14127
cell division regulator GpsB;
3-48 4.60e-10

cell division regulator GpsB;


Pssm-ID: 237616 [Multi-domain]  Cd Length: 109  Bit Score: 55.40  E-value: 4.60e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489736755   3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQE 48
Cdd:PRK14127   6 LTPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYEAFQKEIEELQQ 51
growth_prot_Scy NF041483
polarized growth protein Scy;
47-152 2.48e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 38.65  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755   47 QERLDSSEGKLKYFNELKDSLNQSILVAQEAADKVKTNSKKEADIITREAQKQASDIVSEATDKSNQMIDEASQKAKRLS 126
Cdd:NF041483 1030 KRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELL 1109

                          90       100
                  ....*....|....*....|....*.
gi 489736755  127 VETDDLKKQTRVFRQRLQVMLESQLE 152
Cdd:NF041483 1110 VGARRDATAIRERAEELRDRITGEIE 1135
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 57-154 9.17e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 35.11  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755  57 LKYFNELKDSLNQSILVAQEAADKVKtNSKKEADIITREAQKQASDIVSEATDKSNQMIDEASQKAKRlsvETDDLKKQT 136
Cdd:cd06503   25 LKALDEREEKIAESLEEAEKAKEEAE-ELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKE---EAERILEQA 100

                         90       100
                 ....*....|....*....|
gi 489736755 137 R--VFRQRLQVMLESQLEVV 154
Cdd:cd06503  101 KaeIEQEKEKALAELRKEVA 120
 
Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 3-144 8.45e-47

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 151.18  E-value: 8.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755    3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQERLDSSEGKLKYFNELKDSLNQSILVAQEAADKVK 82
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489736755   83 TNSKKEADIITREAQKQAsdivseatdksNQMIDEASQKAKRLSVETDDLKKQTRVFRQRLQ 144
Cdd:pfam05103  81 ANAQKEAELIIKEAEAKA-----------ERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1-136 1.21e-41

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 138.06  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755   1 MVLSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQERLDSSEGKLKYFNELKDSLNQSILVAQEAADK 80
Cdd:COG3599    1 MKLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489736755  81 VKTNSKKEADIITREAQKQASDIVSEATDKSNQMIDeasqkakrlsvETDDLKKQT 136
Cdd:COG3599   81 VKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVR-----------EIEELKRQR 125
DivI1A_domain TIGR03544
DivIVA domain; This model describes a domain found in Bacillus subtilis cell division ...
 3-36 2.31e-12

DivIVA domain; This model describes a domain found in Bacillus subtilis cell division initiation protein DivIVA, and homologs, toward the N-terminus. It is also found as a repeated domain in certain other proteins, including family TIGR03543.


Pssm-ID: 274639 [Multi-domain]  Cd Length: 34  Bit Score: 59.36  E-value: 2.31e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489736755    3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDY 36
Cdd:TIGR03544   1 LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL 34
PRK14127 PRK14127
cell division regulator GpsB;
3-48 4.60e-10

cell division regulator GpsB;


Pssm-ID: 237616 [Multi-domain]  Cd Length: 109  Bit Score: 55.40  E-value: 4.60e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489736755   3 LSPDDIHNKEFSTKLRGYNIDEVNDFLEQIIKDYQITLKQNKDLQE 48
Cdd:PRK14127   6 LTPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYEAFQKEIEELQQ 51
PRK01005 PRK01005
V-type ATP synthase subunit E; Provisional
 52-151 1.21e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179204 [Multi-domain]  Cd Length: 207  Bit Score: 38.61  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755  52 SSEGKLKyfnELKDSLN-QSILVAQEAADKVKTNSKKEADIITREAQKQASDIVSEATDKSNQMIDE---ASQKAKRLSV 127
Cdd:PRK01005   5 SAQDKLK---QICDALReETLKPAEEEAGAIVHNAKEQAKRIIAEAQEEAEKIIRSAEETADQKLKQgesALVQAGKRSL 81

                         90       100
                 ....*....|....*....|....
gi 489736755 128 ETDDLKKQTRVFRQRLQVMLESQL 151
Cdd:PRK01005  82 ESLKQAVENKIFRESLGEWLEHVL 105
growth_prot_Scy NF041483
polarized growth protein Scy;
47-152 2.48e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 38.65  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755   47 QERLDSSEGKLKYFNELKDSLNQSILVAQEAADKVKTNSKKEADIITREAQKQASDIVSEATDKSNQMIDEASQKAKRLS 126
Cdd:NF041483 1030 KRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELL 1109

                          90       100
                  ....*....|....*....|....*.
gi 489736755  127 VETDDLKKQTRVFRQRLQVMLESQLE 152
Cdd:NF041483 1110 VGARRDATAIRERAEELRDRITGEIE 1135
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 57-154 9.17e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 35.11  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736755  57 LKYFNELKDSLNQSILVAQEAADKVKtNSKKEADIITREAQKQASDIVSEATDKSNQMIDEASQKAKRlsvETDDLKKQT 136
Cdd:cd06503   25 LKALDEREEKIAESLEEAEKAKEEAE-ELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKE---EAERILEQA 100

                         90       100
                 ....*....|....*....|
gi 489736755 137 R--VFRQRLQVMLESQLEVV 154
Cdd:cd06503  101 KaeIEQEKEKALAELRKEVA 120
 
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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