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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004237000
- symbol?: lytH
- synonym:
- description?: N-acetylmuramoyl-L-alanine amidase
- N-acetylmuramoyl-L-alanine amidase
- cell wall amidase
- SH3 domain-containing protein
- cell wall amidase lytH
- cell wall hydrolase/autolysin
- LytH protein involved in methicillin resistance / N-acetylmuramoyl-L-alanine amidase domain protein
- N-acetylmuramoyl-L-alanine amidase family protein
- pseudogene
- putative N-acetylmuramoyl-L-alanine amidase
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4482932..4483744
- synteny block?: BlockID0032650
- occurrence?: in 100% of 34 strains
lytH : peptidoglycan stem peptide-trimming endopeptidase LytH [1]
• A crystal structure is available: 7TJ4
- Staphylocci produce multiple cell wall remodeling enzymes that differ in where they digest peptidoglycan, their localization on the membrane and regulation of their activity
- Staphylococci produce one bifunctional N-acetylglucosaminidase/amidase: Atl (AtlA)
- Staphylococci produce three N-acetylglucosaminidases: SagA (LytD, AtlE), SagB and ScaH (Aly)
- Staphylococci produce two bifunctional amidase/endopeptidases: LytN and EssH
- Staphylococci produce two lytic transglycosylases: SceD and IsaA
- Staphylococci produce two monofunctional amidases: SsaA and Sle1
- Staphylococci produce three monofunctional endopeptidases: LytH, LytM and LytU
- Staphylococci produce five uncharacterized probable monofunctional amidases: (SsaA2), (SsaA3), (SsaA4), (SsaA5) and (SsaA6)
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1590 (lytH)
08BA02176:
C248_1675 (lytH)
11819-97:
MS7_1647
6850:
RSAU_001493 (lytH)
71193:
ST398NM01_1695
ECT-R 2:
ECTR2_1480
ED133:
SAOV_1629
ED98:
SAAV_1625
HO 5096 0412:
SAEMRSA15_15490
JH1:
SaurJH1_1722
JH9:
SaurJH9_1689
JKD6008:
SAA6008_01601 (lytH)
JKD6159:
SAA6159_01564 (lytH)
JSNZ:
JSNZ_001622
LGA251:
SARLGA251_15340
M013:
M013TW_1652
MRSA252:
SAR1712
MSHR1132:
SAMSHR1132_14680
MSSA476:
SAS1568
Mu3:
SAHV_1619 (lytH)
Mu50:
SAV1632 (lytH)
MW2:
MW1582
RF122:
SAB1501c
ST398:
SAPIG1695 (lytH)
T0131:
SAT0131_01730 (sdrE)
TCH60:
HMPREF0772_11510 (amiD5)
TW20:
SATW20_16260
USA300_TCH1516:
USA300HOU_1630 (lytH)
VC40:
SAVC_07405
⊟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 MKKIEAWLSKKGLKNKRTLIVVIAFVLFIIFLFLLLNSNSEDSGNITITENAELRTGPNA
N315 MKKIEAWLSKKGLKNKRTLIVVIAFVLFIIFLFLLLNSNSEDSGNITITENAELRTGPNA
NCTC8325 MKKIEAWLSKKGLKNKRTLIVVIAFVLFIIFLFLLLNSNSEDSGNITITENAELRTGPNA
Newman MKKIEAWLSKKGLKNKRTLIVVIAFVLFIIFLFLLLNSNSEDSGNITITENAELRTGPNA
USA300_FPR3757 MKKIEAWLSKKGLKNKRTLIVVIAFVLFIIFLFLLLNSNSEDSGNITITENAELRTGPNA
************************************************************
COL AYPVIYKVEKGDHFKKIGKVGKWIEVEDTSSNEKGWIAGWHTNLDIVADNTKEKNPLQGK
N315 AYPVIYKVEKGDHFKKIGKVGKWIEVEDTSSNEKGWIAGWHTNLDIVADNTKEKNPLQGK
NCTC8325 AYPVIYKVEKGDHFKKIGKVGKWIEVEDTSSNEKGWIAGWHTNLDIVADNTKEKNPLQGK
Newman AYPVIYKVEKGDHFKKIGKVGKWIEVEDTSSNEKGWIAGWHTNLDIVADNTKEKNPLQGK
USA300_FPR3757 AYPVIYKVEKGDHFKKIGKVGKWIEVEDTSSNEKGWIAGWHTNLDIVADNTKEKNPLQGK
************************************************************
COL TIVLDPGHGGSDQGASSNTKYKSLEKDYTLKTAKELQRTLEKEGATVKMTRTDDTYVSLE
N315 TIVLDPGHGGSDQGASSNTKYKSLEKDYTLKTAKELQRTLEKEGATVKMTRTDDTYVSLE
NCTC8325 TIVLDPGHGGSDQGASSNTKYKSLEKDYTLKTAKELQRTLEKEGATVKMTRTDDTYVSLE
Newman TIVLDPGHGGSDQGASSNTKYKSLEKDYTLKTAKELQRTLEKEGATVKMTRTDDTYVSLE
USA300_FPR3757 TIVLDPGHGGSDQGASSNTKYKSLEKDYTLKTAKELQRTLEKEGATVKMTRTDDTYVSLE
************************************************************
COL NRDIKGDAYLSIHNDALESSNANGMTVYWYHDNQRALADTLDATIQKKGLLSNRGSRQEN
N315 NRDIKGDAYLSIHNDALESSNANGMTVYWYHDNQRALADTLDATIQKKGLLSNRGSRQEN
NCTC8325 NRDIKGDAYLSIHNDALESSNANGMTVYWYHDNQRALADTLDATIQKKGLLSNRGSRQEN
Newman NRDIKGDAYLSIHNDALESSNANGMTVYWYHDNQRALADTLDATIQKKGLLSNRGSRQEN
USA300_FPR3757 NRDIKGDAYLSIHNDALESSNANGMTVYWYHDNQRALADTLDATIQKKGLLSNRGSRQEN
************************************************************
COL YQVLRQTKVPAVLLELGYISNPTDETMIKDQLHRQILEQAIVDGLKIYFSA
N315 YQVLRQTKVPAVLLELGYISNPTDETMIKDQLHRQILEQAIVDGLKIYFSA
NCTC8325 YQVLRQTKVPAVLLELGYISNPTDETMIKDQLHRQILEQAIVDGLKIYFSA
Newman YQVLRQTKVPAVLLELGYISNPTDETMIKDQLHRQILEQAIVDGLKIYFSA
USA300_FPR3757 YQVLRQTKVPAVLLELGYISNPTDETMIKDQLHRQILEQAIVDGLKIYFSA
***************************************************
- ↑ Min Wang, Girbe Buist, Jan Maarten van Dijl
Staphylococcus aureus cell wall maintenance - the multifaceted roles of peptidoglycan hydrolases in bacterial growth, fitness, and virulence.
FEMS Microbiol Rev: 2022, 46(5);
[PubMed:35675307] [WorldCat.org] [DOI] (I p)Min Wang, Xiaofang Li, Francis M Cavallo, Harita Yedavally, Sjouke Piersma, Elisa J M Raineri, Elias Vera Murguia, Jeroen Kuipers, Zhenhua Zhang, Jan Maarten van Dijl, Girbe Buist
Functional profiling of CHAP domain-containing peptidoglycan hydrolases of Staphylococcus aureus USA300 uncovers potential targets for anti-staphylococcal therapies.
Int J Med Microbiol: 2024, 316;151632
[PubMed:39142057] [WorldCat.org] [DOI] (I p)Takaji Fujimura, Kazuhisa Murakami
Staphylococcus aureus clinical isolate with high-level methicillin resistance with an lytH mutation caused by IS1182 insertion.
Antimicrob Agents Chemother: 2008, 52(2);643-7
[PubMed:18070966] [WorldCat.org] [DOI] (P p)Truc Do, Kaitlin Schaefer, Ace George Santiago, Kathryn A Coe, Pedro B Fernandes, Daniel Kahne, Mariana G Pinho, Suzanne Walker
Staphylococcus aureus cell growth and division are regulated by an amidase that trims peptides from uncrosslinked peptidoglycan.
Nat Microbiol: 2020, 5(2);291-303
[PubMed:31932712] [WorldCat.org] [DOI] (I p)