ID B9EBS1_MACCJ Unreviewed; 1070 AA.
AC B9EBS1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Probable transglycosylase IsaA {ECO:0000256|ARBA:ARBA00014134};
DE EC=3.4.24.75 {ECO:0000256|ARBA:ARBA00012322};
DE AltName: Full=Immunodominant staphylococcal antigen A {ECO:0000256|ARBA:ARBA00032268};
GN OrderedLocusNames=MCCL_0975 {ECO:0000313|EMBL:BAH17682.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17682.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17682.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17682.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
CC -!- FUNCTION: Is able to cleave peptidoglycan.
CC {ECO:0000256|ARBA:ARBA00003270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-
CC peptide link joining staphylococcal cell wall peptidoglycans.;
CC EC=3.4.24.75; Evidence={ECO:0000256|ARBA:ARBA00001667};
CC -!- SIMILARITY: Belongs to the peptidase M23B family.
CC {ECO:0000256|ARBA:ARBA00006646}.
CC -!- SIMILARITY: Belongs to the transglycosylase family. IsaA subfamily.
CC {ECO:0000256|ARBA:ARBA00006406}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009484; BAH17682.1; -; Genomic_DNA.
DR RefSeq; WP_012656882.1; NC_011999.1.
DR AlphaFoldDB; B9EBS1; -.
DR STRING; 458233.MCCL_0975; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR KEGG; mcl:MCCL_0975; -.
DR eggNOG; COG0739; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG3953; Bacteria.
DR HOGENOM; CLU_287685_0_0_9; -.
DR OrthoDB; 28713at2; -.
DR Proteomes; UP000001383; Chromosome.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01551; Peptidase_M23; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000001383}.
FT DOMAIN 459..502
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 912..955
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT COILED 615..733
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1070 AA; 116421 MW; 5A9C1D5FFA4FA753 CRC64;
MPKGTHVYNN KQTEELLEPA RYSRGTPGMG MLVKATSNAI TSSTKLFGAK NTRKALDYTA
EKGAEVEKVT RAGAEIAGDI MDYIENPSKL VDLAMKKFGV DFSGISGLPG DMMLSAYKKL
KNQTVKLVTG WIDEATGGNA DGTEILGWPM TTPYSPNAAV PGYPTSFNGG RHYGIDLGIP
SGTTIHAPTS GIVSQQSNYG GGMVARLLSG KIAQYFLHLS KVLKTGPVKQ GDAIAKSGNS
GAWTTGAHLH YQVESPASAE LTNANTLDPV KFLKGKGGGG AGILKSVSAP GNISNWISSA
IKRTSVPSTW APYLKTIAKY ESGFNPAAVQ NGYVDVNTGG NEARGLMQVT PQTYRGLMGT
TEGMMNPINN ITASIKWIKS RYGTVTNIPG MASGTWRGGY ANGGIIPKDS IYRGGEEGKE
VVIPTVPKRK NRANQLIALA DRMVNGKPKR YAGGTKKPST HKVKWGDTLW DISRKNGTTV
KALQLLNGIK NHLIYPGQII KLTGAITGLK KNVSQQSKTH KATVQALSKA QRMYNTGSAI
AKRGKTSGKV TGKEDIAIGN LIMANMKNIG KLPVEKMQSN LNAINKKINS VIASNEGKIA
TLNNKIVKSS KSAEIKGASR EIQNRKNNIA TLNSKIKKTS NKKLIAKYKK DIKAHQRKIS
SLENKIKRAT NNKVANNARA DIAAYQAQIN SLKKLKQSEV LKTNFLDSLV KHKQRLQNQL
NKKNEERKAL TESKMSFRDS IRDSYRGLAG FEAAKGNTSK DFIAFMKYRL NRMKKFAANV
SKLRQMGLDP TILREILAGG IETAIPRVET LVGGGKKNVL EINKLQKQVL SYVNNLSNEH
SRFGYDNEIK AKDKEVSSIK KQQISLQSRA TSYLTAKPKT KPKVKPKALV KKTVASKVKA
KVTPKAKPKK TRTHNIKWGD TLGGIAAKYH TSVSAIKKLN GLKSDMIYAG RKLKIPGYAK
GGIVNIPQIA WIAEGGFAES IISHDPSQRV QQQKIWKDTG DKLGFTKDDA LTMRMIQLLE
EQREIQRAIA QRDTVLQMDG KAVGKQIAPH IDKELARIME LGKRGVRHGG
//
