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Database: UniProt
Entry: A0A081XN59_STRTO
LinkDB: A0A081XN59_STRTO
Original site: A0A081XN59_STRTO 
ID   A0A081XN59_STRTO        Unreviewed;      1066 AA.
AC   A0A081XN59;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Peptidase M28 {ECO:0000313|EMBL:KES04982.1};
GN   ORFNames=BU52_22425 {ECO:0000313|EMBL:KES04982.1};
OS   Streptomyces toyocaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=55952 {ECO:0000313|EMBL:KES04982.1, ECO:0000313|Proteomes:UP000028341};
RN   [1] {ECO:0000313|EMBL:KES04982.1, ECO:0000313|Proteomes:UP000028341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15009 {ECO:0000313|EMBL:KES04982.1,
RC   ECO:0000313|Proteomes:UP000028341};
RA   Hong H.-J., Kwun M.J.;
RT   "The genome announcement of Streptomyces toyocaensis NRRL15009.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KES04982.1}.
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DR   EMBL; JFCB01000021; KES04982.1; -; Genomic_DNA.
DR   RefSeq; WP_037937007.1; NZ_JFCB01000021.1.
DR   AlphaFoldDB; A0A081XN59; -.
DR   STRING; 55952.BU52_22425; -.
DR   eggNOG; COG2234; Bacteria.
DR   eggNOG; COG3227; Bacteria.
DR   OrthoDB; 345880at2; -.
DR   Proteomes; UP000028341; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd12214; ChiA1_BD; 1.
DR   CDD; cd03876; M28_SGAP_like; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR041756; M28_SGAP-like.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028341};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1066
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001766733"
FT   DOMAIN          1020..1066
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000259|SMART:SM00495"
SQ   SEQUENCE   1066 AA;  110130 MW;  A7E678EF6D71E569 CRC64;
     MLRKMAVAGI SLAMTLGGVT LPASLASAAP AAAPPTSQPK PTPAALAIAA ADQATHSGVD
     ALAKGPDEQY DRSQVTPWTK DLYSVAYERT YKGLPVVGGD AVVLADGKGK VRAVQSAADV
     TITVPTRPKV TQAQAVRTSR AKLAKVEKLD SKRLVVRVKN DHATLAWEAV LTGRTKADVP
     SRLHVFVDAR TGKVVDTYDD VRAGTGHSEW NGPDPLTIDT SRSGSDYVLR DTTRPGLQCS
     DYSGGLFTKS RDDWGTGNAS SKETGCVDAM FAAQKESDML KNWLGRNGHN GNGGSWPVRV
     GLNQLNAYWD GSTVTIGRNS AGKWIAGMDV IGHEFGHGLD SNTPGGANNE SGLGEATGDI
     MGALTEAYTN QPVPYDTPDY TVGEEIDLQG RGPIRNMYNP GALNHPACYS SAIPSTEEHA
     AAGPLNHWFY LLAEGSNPGG GKPSSATCDG STVTGIGIRN AGKIFYGGML LKTSGMTHKR
     YRTATLTAAK NLDASCDLFN TTKAAWNAID VPAQPADPTC TGQQNDFSLA LSAATGDVDA
     GSSVRTTVDT TTVAGGAQQI SLTASGQPAG VDVSFSPATV TSGSSSTMTV SASSGTTRGT
     YVITVTGSAG TKTHTAQYTL RVGGGGDNQP TPPDVDVAKV QAHLSQLHGI AQQNGGNRHA
     TGAGYRASLA YVKGKLQAAG YTVTEQACAS GCSTGAGSNL IAEWPKGNAD NVYMFGAHLD
     GVAAGPGIND NGSGSAALLE TALTLAQSDA TMKNRVRFAW WTDEEAGLNG SDYYTRTLSS
     AERSKIKVYY NFDMVASTNG GYFINNLNSA ASAPMKAYWD SLGLAPQENI EGQGRSDDYS
     FQSIGIPTSG YATGASARKS VAEAAKWGGT AGSAYDPCYH SACDTTSNIS ATALNRSADG
     MAYTIWKTAV AGDPTPANDF SISASPSAGT VAPGTSATVT VSTTTTSGSA QNVRLSASGE
     PTGVTVSFNP SSMTSGQSST ATVQVAAGTP GGTYTLTFTG AGEVSHATTY TLTVSGDGGE
     TTWQLGATYA AGDVVTYNGV RYRCIQGHTA YPGWEPPNVP ALWERV
//
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