ID   CWBA_BACSU              Reviewed;         705 AA.
AC   Q02113;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Amidase enhancer;
DE   AltName: Full=Cell wall-associated polypeptide CWBP76;
DE            Short=CWBP76;
DE   AltName: Full=Modifier protein of major autolysin;
DE   Flags: Precursor;
GN   Name=lytB; Synonyms=cwbA; OrderedLocusNames=BSU35630;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1356138; DOI=10.1099/00221287-138-6-1067;
RA   Kuroda A., Rashid H.M., Sekiguchi J.;
RT   "Molecular cloning and sequencing of the upstream region of the major
RT   Bacillus subtilis autolysin gene: a modifier protein exhibiting sequence
RT   homology to the major autolysin and the spoIID product.";
RL   J. Gen. Microbiol. 138:1067-1076(1992).
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   INDUCTION, AND SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Possibly involved in cell wall metabolism during spore
CC       formation. Enhances the amidase activity approximately threefold.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11987133};
CC       Peripheral membrane protein {ECO:0000269|PubMed:11987133}. Secreted,
CC       cell wall {ECO:0000269|PubMed:11987133}. Note=Cell wall localization
CC       shown in PubMed:11987133.
CC   -!- INDUCTION: In stationary phase; under control of SigD
CC       (PubMed:11987133). Repressed by LytR. {ECO:0000269|PubMed:11987133,
CC       ECO:0000269|PubMed:1357079}.
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DR   EMBL; M87645; AAA22580.1; -; Genomic_DNA.
DR   EMBL; D10388; BAA01224.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15580.1; -; Genomic_DNA.
DR   PIR; A41322; A41322.
DR   RefSeq; NP_391443.1; NC_000964.3.
DR   RefSeq; WP_003243620.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; Q02113; -.
DR   SMR; Q02113; -.
DR   STRING; 224308.BSU35630; -.
DR   jPOST; Q02113; -.
DR   PaxDb; Q02113; -.
DR   PRIDE; Q02113; -.
DR   EnsemblBacteria; CAB15580; CAB15580; BSU_35630.
DR   GeneID; 936795; -.
DR   KEGG; bsu:BSU35630; -.
DR   PATRIC; fig|224308.179.peg.3854; -.
DR   eggNOG; COG2247; Bacteria.
DR   eggNOG; COG2385; Bacteria.
DR   InParanoid; Q02113; -.
DR   OMA; WILKNKE; -.
DR   BioCyc; BSUB:BSU35630-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR   InterPro; IPR007253; Cell_wall-bd_2.
DR   InterPro; IPR013486; SpoIID/LytB.
DR   InterPro; IPR013693; SpoIID/LytB_N.
DR   Pfam; PF04122; CW_binding_2; 3.
DR   Pfam; PF08486; SpoIID; 1.
DR   TIGRFAMs; TIGR02669; SpoIID_LytB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Membrane; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:11987133"
FT   CHAIN           26..705
FT                   /note="Amidase enhancer"
FT                   /id="PRO_0000021051"
FT   REPEAT          64..161
FT                   /note="1"
FT   REPEAT          162..251
FT                   /note="2"
FT   REPEAT          252..349
FT                   /note="3"
FT   REGION          64..349
FT                   /note="3 X tandem repeats"
SQ   SEQUENCE   705 AA;  76729 MW;  A1A2449C2D801528 CRC64;
     MKSCKQLIVC SLAAILLLIP SVSFAADSNI SVKLLNYIGN KSSISLSPTG FYKVTGDNVA
     VTDRFAGASR YETATLASNS QWKNPNTVIL VNRDIFIDAL PVIPLAKKLN APVLFTQPDT
     LTKTTERQIA KFNPDNILII GGARSISKDV ENKLKSYGAV KRISGKNRYV LSENIAKQMG
     SYDKAIVVTG RVFQDALAIA PYAAAHGYPI LLTEKDKLPD YDLPKQVIII GSSFSVSDSV
     ENQIKKTSTV QRIPGSTRYE LTANIIKQLK LKADKVVMTN GTKYADVLIG ASLASKKNSQ
     ILFVKQDSVP AAAKSITKDK ATYAYDFIGS TSSISAEVEN SLADEFYLAD GGTYNLKINS
     GKLNLENIKT YGNSLRIKPE NYSTSNRISL DGKQYLGTVN FSIESTKYIR PVNENIPFED
     YLKGVIPNEM PASWSLEALK AQTVAARTYS ITKTGTTVPD TTAFQVYGGY SWNSNTNKAV
     EQTKGKVLKY NGSLITAAYS SSNGGYTEAS NEVWSSSVPY LIAKKDTKDP QIGWTLTLSK
     QQLDTKSLDL TKPSSWWSSA TETDSARLSG VKNWILKNKE TSADSVKIAS IDDLSFSGTT
     QGQRAKTASM KVKYFVKSST GSYNLSKITT ISVPTSELRT MIGATVFKST YVTVKKDTSK
     YTISGKGYGH GIGMSQYGAK ARAEAGDSYS SILKFYYPGT TLTSY