LYTC_BACSU
ID LYTC_BACSU Reviewed; 496 AA.
AC Q02114;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase LytC;
DE EC=3.5.1.28;
DE AltName: Full=Cell wall-associated polypeptide CWBP49;
DE Short=CWBP49;
DE AltName: Full=Major autolysin;
DE AltName: Full=Vegetative cell wall hydrolase LytC;
DE Flags: Precursor;
GN Name=lytC; Synonyms=cwlB; OrderedLocusNames=BSU35620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REPRESSION BY LYTR.
RC STRAIN=168;
RX PubMed=1357079; DOI=10.1099/00221287-138-9-1949;
RA Lazarevic V., Margot P., Soldo B., Karamata D.;
RT "Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a
RT regulatory unit encompassing the structural genes of the N-acetylmuramoyl-
RT L-alanine amidase and its modifier.";
RL J. Gen. Microbiol. 138:1949-1961(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44 AND 297-309,
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=168;
RX PubMed=1682302; DOI=10.1128/jb.173.22.7304-7312.1991;
RA Kuroda A., Sekiguchi J.;
RT "Molecular cloning and sequencing of a major Bacillus subtilis autolysin
RT gene.";
RL J. Bacteriol. 173:7304-7312(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=11987133;
RX DOI=10.1002/1615-9861(200205)2:5<591::aid-prot591>3.0.co;2-8;
RA Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.;
RT "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic
RT approach.";
RL Proteomics 2:591-602(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / AC327;
RX PubMed=8405954; DOI=10.1111/j.1574-6968.1993.tb06438.x;
RA Rashid M.H., Kuroda A., Sekiguchi J.;
RT "Bacillus subtilis mutant deficient in the major autolytic amidase and
RT glucosaminidase is impaired in motility.";
RL FEMS Microbiol. Lett. 112:135-140(1993).
RN [6]
RP INDUCTION.
RC STRAIN=168 / AC327;
RX PubMed=8093697; DOI=10.1128/jb.175.3.795-801.1993;
RA Kuroda A., Sekiguchi J.;
RT "High-level transcription of the major Bacillus subtilis autolysin operon
RT depends on expression of the sigma D gene and is affected by a sin (flaD)
RT mutation.";
RL J. Bacteriol. 175:795-801(1993).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=14594841; DOI=10.1128/jb.185.22.6666-6677.2003;
RA Yamamoto H., Kurosawa S., Sekiguchi J.;
RT "Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF
RT on the Bacillus subtilis cell surface and stability of these enzymes to
RT cell wall-bound or extracellular proteases.";
RL J. Bacteriol. 185:6666-6677(2003).
RN [8]
RP REPRESSION BY YVRH.
RC STRAIN=168;
RX PubMed=16306698; DOI=10.1271/bbb.69.2155;
RA Serizawa M., Kodama K., Yamamoto H., Kobayashi K., Ogasawara N.,
RA Sekiguchi J.;
RT "Functional analysis of the YvrGHb two-component system of Bacillus
RT subtilis: identification of the regulated genes by DNA microarray and
RT northern blot analyses.";
RL Biosci. Biotechnol. Biochem. 69:2155-2169(2005).
RN [9]
RP FUNCTION IN SWARMING MOTILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79, and 3610;
RX PubMed=19542270; DOI=10.1128/jb.00521-09;
RA Chen R., Guttenplan S.B., Blair K.M., Kearns D.B.;
RT "Role of the sigmaD-dependent autolysins in Bacillus subtilis population
RT heterogeneity.";
RL J. Bacteriol. 191:5775-5784(2009).
CC -!- FUNCTION: Autolysins are cell wall hydrolases involved in some
CC important biological processes such as cell separation, cell-wall
CC turnover, competence for genetic transformation, formation of the
CC flagella - in particular of its basal body - and sporulation. Has a
CC high affinity for teichoic acid-endowed peptidoglycan. LytC is required
CC for efficient swarming motility but not at the level of cell separation
CC or flagellum biosynthesis. Rather, LytC appears to be important for
CC proper flagellar function. {ECO:0000269|PubMed:1682302,
CC ECO:0000269|PubMed:19542270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000269|PubMed:1682302};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11987133,
CC ECO:0000269|PubMed:14594841, ECO:0000269|PubMed:1682302}. Note=LytC
CC localizes uniformly to the cell wall, into which the peritrichous
CC flagella are randomly inserted.
CC -!- INDUCTION: Expressed under the control of SigD (major), the transcripts
CC being predominants at the exponential growth phase, and SigA (minor).
CC Repressed by LytR and YvrH. {ECO:0000269|PubMed:11987133,
CC ECO:0000269|PubMed:1357079, ECO:0000269|PubMed:16306698,
CC ECO:0000269|PubMed:8093697}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene leads to an
CC approximately 90% decrease in the total cell wall hydrolytic activity
CC of stationary-phase cells and extraordinary resistance to cell lysis,
CC even after 6 days of incubation at 37 degrees Celsius. Cells from
CC domesticated laboratory strains lacking this gene show no motility
CC changes on swarm plates; however in combination with an
CC acetylglucosaminidase deletion (lytD, AC P39848) greatly reduced
CC motility is seen. They also show no apparent changes in cell
CC morphology, competence, sporulation, or germination. Cells from an
CC undomesticated strain (3610) lacking this gene show a reduction in the
CC rate of swarming motility. {ECO:0000269|PubMed:1682302,
CC ECO:0000269|PubMed:19542270, ECO:0000269|PubMed:8405954}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
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DR EMBL; M87645; AAA22581.1; -; Genomic_DNA.
DR EMBL; M81324; AAA22371.1; -; Genomic_DNA.
DR EMBL; D10388; BAA01225.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15579.1; -; Genomic_DNA.
DR PIR; B41322; B41322.
DR RefSeq; NP_391442.1; NC_000964.3.
DR RefSeq; WP_003242758.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; Q02114; -.
DR SMR; Q02114; -.
DR STRING; 224308.BSU35620; -.
DR jPOST; Q02114; -.
DR PaxDb; Q02114; -.
DR PRIDE; Q02114; -.
DR EnsemblBacteria; CAB15579; CAB15579; BSU_35620.
DR GeneID; 936777; -.
DR KEGG; bsu:BSU35620; -.
DR PATRIC; fig|224308.179.peg.3853; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG2247; Bacteria.
DR OMA; LANCDNF; -.
DR PhylomeDB; Q02114; -.
DR BioCyc; BSUB:BSU35620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF04122; CW_binding_2; 3.
DR SMART; SM00646; Ami_3; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:11987133,
FT ECO:0000269|PubMed:1682302"
FT CHAIN 25..496
FT /note="N-acetylmuramoyl-L-alanine amidase LytC"
FT /id="PRO_0000006459"
FT REPEAT 30..128
FT /note="1"
FT REPEAT 129..222
FT /note="2"
FT REPEAT 223..318
FT /note="3"
FT DOMAIN 322..490
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
FT REGION 30..318
FT /note="3 X tandem repeats"
SQ SEQUENCE 496 AA; 52626 MW; 146FF36B41BB5EC5 CRC64;
MRSYIKVLTM CFLGLILFVP TALADNSVKR VGGSNRYGTA VQISKQMYST ASTAVIVGGS
SYADAISAAP LAYQKNAPLL YTNSDKLSYE TKTRLKEMQT KNVIIVGGTP AVSSNTANQI
KSLGISIKRI AGSNRYDTAA RVAKAMGATS KAVILNGFLY ADAPAVIPYA AKNGYPILFT
NKTSINSATT SVIKDKGISS TVVVGGTGSI SNTVYNKLPS PTRISGSNRY ELAANIVQKL
NLSTSTVYVS NGFSYPDSIA GATLAAKKKQ SLILTNGENL STGARKIIGS KNMSNFMIIG
NTPAVSTKVA NQLKNPVVGE TIFIDPGHGD QDSGAIGNGL LEKEVNLDIA KRVNTKLNAS
GALPVLSRSN DTFYSLQERV NKAASAQADL FLSIHANAND SSSPNGSETY YDTTYQAANS
KRLAEQIQPK LAANLGTRDR GVKTAAFYVI KYSKMPSVLV ETAFITNASD ASKLKQAVYK
DKAAQAIHDG TVSYYR
