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   27-MAR-2024, entry version 147.
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; Bacillota; 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; 224308-BSU35620; -.
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   InParanoid; Q02114; -.
DR   OrthoDB; 363232at2; -.
DR   PhylomeDB; Q02114; -.
DR   BioCyc; BSUB:BSU35620-MONOMER; -.
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   Gene3D; 3.40.50.12090; -; 2.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR007253; Cell_wall-bd_2.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30032:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE CWLM; 1.
DR   PANTHER; PTHR30032; N-ACETYLMURAMOYL-L-ALANINE AMIDASE-RELATED; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF04122; CW_binding_2; 3.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 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
//