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Conserved domains on  [gi|896620700|ref|WP_049502424|]
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DivIVA domain-containing protein [Streptococcus mitis]

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 5.83e-40

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: 135.77  E-value: 5.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700    3 ITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYEDLVRSNHDKDLHIKSLEERLSYFDEMKDSLSQSVLIAQDTAERVK 82
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896620700   83 qaatersnniiQQAEQDAQRLLEEAKYKANEILRQATDNAKKVAVETEELKNKSRVFHQRLK 144
Cdd:pfam05103  81 -----------ANAQKEAELIIKEAEAKAERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
 
Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 3-144 5.83e-40

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: 135.77  E-value: 5.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700    3 ITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYEDLVRSNHDKDLHIKSLEERLSYFDEMKDSLSQSVLIAQDTAERVK 82
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896620700   83 qaatersnniiQQAEQDAQRLLEEAKYKANEILRQATDNAKKVAVETEELKNKSRVFHQRLK 144
Cdd:pfam05103  81 -----------ANAQKEAELIIKEAEAKAERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1-120 1.15e-35

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: 124.58  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700   1 MPITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYEDLVRSNHDKDLHIKSLEERLSYFDEMKDSLSQSVLIAQDTAER 80
Cdd:COG3599    1 MKLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 896620700  81 VKQAATERSNNIIQQAEQDAQRLLEEAKYKANEILRQATD 120
Cdd:COG3599   81 VKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIEE 120
DivI1A_domain TIGR03544
DivIVA domain; This model describes a domain found in Bacillus subtilis cell division ...
 3-36 2.19e-11

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: 57.44  E-value: 2.19e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 896620700    3 ITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDY 36
Cdd:TIGR03544   1 LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL 34
PRK14127 PRK14127
cell division regulator GpsB;
4-37 2.66e-08

cell division regulator GpsB;


Pssm-ID: 237616 [Multi-domain]  Cd Length: 109  Bit Score: 51.17  E-value: 2.66e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 896620700   4 TSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYE 37
Cdd:PRK14127   7 TPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYE 40
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 71-119 1.33e-04

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 42.50  E-value: 1.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 896620700  71 VLIAQDTAERVKQAATERSNNIIQQAEQDAQRLLEEAKYKANEILRQAT 119
Cdd:cd03404  179 VNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAE 227
 
Name Accession Description Interval E-value
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 3-144 5.83e-40

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: 135.77  E-value: 5.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700    3 ITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYEDLVRSNHDKDLHIKSLEERLSYFDEMKDSLSQSVLIAQDTAERVK 82
Cdd:pfam05103   1 LTPLDIQNKEFKKKMRGYDPDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLILAQETAEEVK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896620700   83 qaatersnniiQQAEQDAQRLLEEAKYKANEILRQATDNAKKVAVETEELKNKSRVFHQRLK 144
Cdd:pfam05103  81 -----------ANAQKEAELIIKEAEAKAERIVDDANNEVKKINDEIEELKRQRRQFRTRFK 131
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1-120 1.15e-35

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: 124.58  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700   1 MPITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYEDLVRSNHDKDLHIKSLEERLSYFDEMKDSLSQSVLIAQDTAER 80
Cdd:COG3599    1 MKLTPLDIRNKEFKKGFRGYDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 896620700  81 VKQAATERSNNIIQQAEQDAQRLLEEAKYKANEILRQATD 120
Cdd:COG3599   81 VKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIEE 120
DivI1A_domain TIGR03544
DivIVA domain; This model describes a domain found in Bacillus subtilis cell division ...
 3-36 2.19e-11

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: 57.44  E-value: 2.19e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 896620700    3 ITSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDY 36
Cdd:TIGR03544   1 LTPEDIRNKRFKKKLRGYDAAEVDAFLDRVADDL 34
PRK14127 PRK14127
cell division regulator GpsB;
4-37 2.66e-08

cell division regulator GpsB;


Pssm-ID: 237616 [Multi-domain]  Cd Length: 109  Bit Score: 51.17  E-value: 2.66e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 896620700   4 TSLEIKDKTFSTRFRGFDQEEVDEFLDIVVRDYE 37
Cdd:PRK14127   7 TPKDILEKEFKTSMRGYDQDEVDKFLDDVIKDYE 40
PRK01005 PRK01005
V-type ATP synthase subunit E; Provisional
 74-192 3.53e-05

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179204 [Multi-domain]  Cd Length: 207  Bit Score: 44.00  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700  74 AQDTAERVKQAATERSNNIIQQAEQDAQRLLEEAKYKANEILRQ---ATDNAKKVAVETEELKNKSRVFHQRLKSTIESQ 150
Cdd:PRK01005  25 AEEEAGAIVHNAKEQAKRIIAEAQEEAEKIIRSAEETADQKLKQgesALVQAGKRSLESLKQAVENKIFRESLGEWLEHV 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 896620700 151 L-----------AIVESSDWEDILRPTATYLQTSDEAfkEVVSEVLGDSVLQQ 192
Cdd:PRK01005 105 LtdpevsakliqALVQAIEAQGISGNLTAYIGKHVSA--RAVNELLGKEVTKK 155
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 71-119 1.33e-04

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 42.50  E-value: 1.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 896620700  71 VLIAQDTAERVKQAATERSNNIIQQAEQDAQRLLEEAKYKANEILRQAT 119
Cdd:cd03404  179 VNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAE 227
PRK04132 PRK04132
replication factor C small subunit; Provisional
 50-192 1.02e-03

replication factor C small subunit; Provisional


Pssm-ID: 235223 [Multi-domain]  Cd Length: 846  Bit Score: 40.59  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896620700  50 IKSLEERLSYFDEMKDSLSQSVLIaqDTAErvkqaATERSNNIIQQAEQDAQRLLEEAKYKANEILRQATDNAKKVAVET 129
Cdd:PRK04132 388 MKEIYYRLEELERLKKALSESILI--DWNE-----VAKRRKEIAEKTGIRADRILEYIKGKRKPSLKNYIKIAKALGINL 460

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896620700 130 EELKNKSRVFHQRLKSTIES-QLAIVESSDWEDILRPTATYLQTSDEAFK---EVVSEVLGDSVLQQ 192
Cdd:PRK04132 461 EKTIEAMRIFAKKYSSYAEIgRMLGTWNSSVKIILESNTQEIEKLEEIRKielKLIKEILNDEKLKE 527
 
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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