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⊟Summary[edit | edit source]
- pan ID?: SAUPAN003315000
- symbol?: def
- synonym:
- description?: peptide deformylase
- peptide deformylase
- putative polypeptide deformylase 2
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 3682725..3683276
- synteny block?: BlockID0023990
- occurrence?: in 100% of 34 strains
defB : peptide deformylase [1]
• A crystal structure is available : 1LMH
While all bacterial coding sequences initiate with a formyl-methionine, not all ribosomal proteins contain an N-terminal formyl-methionine. Staphylococci contain two peptide deformylase paralogues whereas most gram-negative bacteria contain only one. Although DefA more closely resembles the Class I peptide deformylase from gram-negative bacteria, it does not remove formate from proteins and its function is unknown. Only the Class II peptide deformylase DefB can remove formate from the N-terminal methionine residues of nascent proteins as they emerge from ribosomes.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1048 (pdf1)
08BA02176:
C248_1118
11819-97:
MS7_1048
6850:
RSAU_000976 (def1)
71193:
ST398NM01_1088
ECT-R 2:
ECTR2_946 (def)
ED133:
SAOV_1035c
ED98:
SAAV_1056 (def)
HO 5096 0412:
SAEMRSA15_09210
JH1:
SaurJH1_1173 (def)
JH9:
SaurJH9_1151 (def)
JKD6008:
SAA6008_01046 (def)
JKD6159:
SAA6159_00947 (def)
JSNZ:
JSNZ_001056 (def)
LGA251:
SARLGA251_10040
M013:
M013TW_1023
MRSA252:
SAR1065 (def)
MSHR1132:
SAMSHR1132_09380
MSSA476:
SAS1026 (def)
Mu3:
SAHV_1083 (def)
Mu50:
SAV1091 (def)
MW2:
MW0974 (def)
RF122:
SAB0957c (def)
ST398:
SAPIG1088 (def)
T0131:
SAT0131_01128
TCH60:
HMPREF0772_12141 (def2)
TW20:
SATW20_10860
USA300_TCH1516:
USA300HOU_1034 (def)
VC40:
SAVC_04615 (def)
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIAKRYGLRSGVG
N315 MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIAKRYGLRSGVG
NCTC8325 MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIAKRYGLRSGVG
Newman MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIAKRYGLRSGVG
USA300_FPR3757 MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIAKRYGLRSGVG
************************************************************
COL LAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSVQEAYLPTGEGCLSVDDNVAG
N315 LAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSVQEAYLPTGEGCLSVDDNVAG
NCTC8325 LAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSVQEAYLPTGEGCLSVDDNVAG
Newman LAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSVQEAYLPTGEGCLSVDDNVAG
USA300_FPR3757 LAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSVQEAYLPTGEGCLSVDDNVAG
************************************************************
COL LVHRHNRITIKAKDIEGNDIQLRLKGYPAIVFQHEIDHLNGVMFYDHIDKDHPLQPHTDA
N315 LVHRHNRITIKAKDIEGNDIQLRLKGYPAIVFQHEIDHLNGVMFYDHIDKNHPLQPHTDA
NCTC8325 LVHRHNRITIKAKDIEGNDIQLRLKGYPAIVFQHEIDHLNGVMFYDHIDKDHPLQPHTDA
Newman LVHRHNRITIKAKDIEGNDIQLRLKGYPAIVFQHEIDHLNGVMFYDHIDKDHPLQPHTDA
USA300_FPR3757 LVHRHNRITIKAKDIEGNDIQLRLKGYPAIVFQHEIDHLNGVMFYDHIDKDHPLQPHTDA
**************************************************:*********
COL VEV
N315 VEV
NCTC8325 VEV
Newman VEV
USA300_FPR3757 VEV
***
- ↑ P S Margolis, C J Hackbarth, D C Young, W Wang, D Chen, Z Yuan, R White, J Trias
Peptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase gene.
Antimicrob Agents Chemother: 2000, 44(7);1825-31
[PubMed:10858337] [WorldCat.org] [DOI] (P p)Eric T Baldwin, Melissa S Harris, Anthony W Yem, Cindy L Wolfe, Anne F Vosters, Kimberly A Curry, Robert W Murray, Jeffrey H Bock, Vincent P Marshall, Joyce I Cialdella, Mahesh H Merchant, Gil Choi, Martin R Deibel
Crystal structure of type II peptide deformylase from Staphylococcus aureus.
J Biol Chem: 2002, 277(34);31163-71
[PubMed:12048187] [WorldCat.org] [DOI] (P p)Andrew N Keller, Xiao Yang, Jana Wiedermannová, Olivier Delumeau, Libor Krásný, Peter J Lewis
ε, a new subunit of RNA polymerase found in gram-positive bacteria.
J Bacteriol: 2014, 196(20);3622-32
[PubMed:25092033] [WorldCat.org] [DOI] (I p)