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Conserved domains on  [gi|1417911069|gb|AWY11376|]
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FemAB family protein, partial [Staphylococcus hominis]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 1-164 2.23e-60

N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase which catalyze the transfer of an acetyl group to a substrate. The mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and then CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member pfam02388:

Pssm-ID: 473072  Cd Length: 406  Bit Score: 192.10  E-value: 2.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417911069   1 TSETKEFSDREDSFYYNRFDHFKDRVLVPLAYIKFDEYLEELHAERQTLNKDLNKALKDIEKRPDNKKAQNKKINLEQQL 80
Cdd:pfam02388 206 TEERRGFHDRSLDYYQDLLDTYGDKAEFMLAYLNFDEYLDKLQEKLNKLQKDLAKLTEALEENPNSKKKKNKLTELKKQL 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417911069  81 KANEQKIDEATQLQLEHGNELPISAGFFFINPFEVVYYAGGTSNKYRHFAGSYAVQWTMINYAIDHGIDRYNFYGISGHF 160
Cdd:pfam02388 286 ASLEKRIGEAQEFIAKDGPVVPLAAALFVYFPQEVVYLYSGSDDKFNKYYAPYLLQWEMIQEAFERGIDRYNFYGIEGDF 365


                  ....
gi 1417911069 161 TDDA 164
Cdd:pfam02388 366 DGSD 369
 
Name Accession Description Interval E-value
FemAB pfam02388
FemAB family; The femAB operon codes for two nearly identical approximately 50-kDa proteins ...
 1-164 2.23e-60

FemAB family; The femAB operon codes for two nearly identical approximately 50-kDa proteins involved in the formation of the Staphylococcal pentaglycine interpeptide bridge in peptidoglycan. These proteins are also considered as a factor influencing the level of methicillin resistance.


Pssm-ID: 426751  Cd Length: 406  Bit Score: 192.10  E-value: 2.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417911069   1 TSETKEFSDREDSFYYNRFDHFKDRVLVPLAYIKFDEYLEELHAERQTLNKDLNKALKDIEKRPDNKKAQNKKINLEQQL 80
Cdd:pfam02388 206 TEERRGFHDRSLDYYQDLLDTYGDKAEFMLAYLNFDEYLDKLQEKLNKLQKDLAKLTEALEENPNSKKKKNKLTELKKQL 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417911069  81 KANEQKIDEATQLQLEHGNELPISAGFFFINPFEVVYYAGGTSNKYRHFAGSYAVQWTMINYAIDHGIDRYNFYGISGHF 160
Cdd:pfam02388 286 ASLEKRIGEAQEFIAKDGPVVPLAAALFVYFPQEVVYLYSGSDDKFNKYYAPYLLQWEMIQEAFERGIDRYNFYGIEGDF 365


                  ....
gi 1417911069 161 TDDA 164
Cdd:pfam02388 366 DGSD 369
FmhB COG2348
Lipid II:glycine glycyltransferase (Peptidoglycan interpeptide bridge formation enzyme) [Cell ...
 96-166 1.15e-20

Lipid II:glycine glycyltransferase (Peptidoglycan interpeptide bridge formation enzyme) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441916 [Multi-domain]  Cd Length: 344  Bit Score: 86.59  E-value: 1.15e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1417911069  96 EHGNElPISAGFFFINPFEVVYYAGGTSNKYRHFAGSYAVQWTMINYAIDHGIDRYNFYGISGHFTDDAED 166
Cdd:COG2348   231 EHEGE-PLAAALVVYSGDEAYYLYGGSSDEYRKLMANYLLQWEAIRWAKERGCTRYDFGGISGDLDPDHPL 300
 
Name Accession Description Interval E-value
FemAB pfam02388
FemAB family; The femAB operon codes for two nearly identical approximately 50-kDa proteins ...
 1-164 2.23e-60

FemAB family; The femAB operon codes for two nearly identical approximately 50-kDa proteins involved in the formation of the Staphylococcal pentaglycine interpeptide bridge in peptidoglycan. These proteins are also considered as a factor influencing the level of methicillin resistance.


Pssm-ID: 426751  Cd Length: 406  Bit Score: 192.10  E-value: 2.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417911069   1 TSETKEFSDREDSFYYNRFDHFKDRVLVPLAYIKFDEYLEELHAERQTLNKDLNKALKDIEKRPDNKKAQNKKINLEQQL 80
Cdd:pfam02388 206 TEERRGFHDRSLDYYQDLLDTYGDKAEFMLAYLNFDEYLDKLQEKLNKLQKDLAKLTEALEENPNSKKKKNKLTELKKQL 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417911069  81 KANEQKIDEATQLQLEHGNELPISAGFFFINPFEVVYYAGGTSNKYRHFAGSYAVQWTMINYAIDHGIDRYNFYGISGHF 160
Cdd:pfam02388 286 ASLEKRIGEAQEFIAKDGPVVPLAAALFVYFPQEVVYLYSGSDDKFNKYYAPYLLQWEMIQEAFERGIDRYNFYGIEGDF 365


                  ....
gi 1417911069 161 TDDA 164
Cdd:pfam02388 366 DGSD 369
FmhB COG2348
Lipid II:glycine glycyltransferase (Peptidoglycan interpeptide bridge formation enzyme) [Cell ...
 96-166 1.15e-20

Lipid II:glycine glycyltransferase (Peptidoglycan interpeptide bridge formation enzyme) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441916 [Multi-domain]  Cd Length: 344  Bit Score: 86.59  E-value: 1.15e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1417911069  96 EHGNElPISAGFFFINPFEVVYYAGGTSNKYRHFAGSYAVQWTMINYAIDHGIDRYNFYGISGHFTDDAED 166
Cdd:COG2348   231 EHEGE-PLAAALVVYSGDEAYYLYGGSSDEYRKLMANYLLQWEAIRWAKERGCTRYDFGGISGDLDPDHPL 300
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 39-92 3.72e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 36.67  E-value: 3.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1417911069  39 LEELHAERQTLNKDLNKALKDIEKRPDNKKAQNKKIN-LEQQLKANEQKIDEATQ 92
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAaLARRIRALEQELAALEA 83
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 39-92 7.08e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 35.96  E-value: 7.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1417911069  39 LEELHAERQTLNKDLNKALKDIEKrpdnkkAQNKKINLEQQLKANEQKIDEATQ 92
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEE------LNEEYNELQAELEALQAEIDKLQA 72
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-93 7.16e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 35.90  E-value: 7.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1417911069  26 VLVPLAYIKFDEYLEELHAERQTLNKDLNKALKDIekrpdnKKAQNKKINLEQQLKANEQKIDEATQL 93
Cdd:COG4942     9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKEL------AALKKEEKALLKQLAALERRIAALARR 70
 
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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