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Database: UniProt
Entry: A0A0U3PV22_9ACTN
LinkDB: A0A0U3PV22_9ACTN
Original site: A0A0U3PV22_9ACTN 
ID   A0A0U3PV22_9ACTN        Unreviewed;       755 AA.
AC   A0A0U3PV22;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Peptidase M4 {ECO:0000313|EMBL:ALV31260.1};
GN   ORFNames=AS200_03715 {ECO:0000313|EMBL:ALV31260.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV31260.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV31260.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV31260.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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DR   EMBL; CP013743; ALV31260.1; -; Genomic_DNA.
DR   RefSeq; WP_058920946.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3PV22; -.
DR   STRING; 1725411.AS200_03715; -.
DR   KEGG; scx:AS200_03715; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000068029; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR023612; Peptidase_M4.
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; PF07504; FTP; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51829; P_HOMO_B; 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:UP000068029};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..755
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006843177"
FT   DOMAIN          629..755
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        367
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        454
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   755 AA;  78490 MW;  CAF4E9F1EAE0BC76 CRC64;
     MPLRPRALLR RRRATALALA SIGSLLSLAV AGHAGAAPAA PSPVKITAKP RAGALPASLT
     PARRAALVKN AQSAAADTAR HLGLGSKEKL LVKDVIRDAD GTTHTRYERT YAGLPVLGGD
     LVVHDKSGLL TVTKAHRGAL SVPSLRSKIS AAGAADRAEA ASKRAEVTGS ETGKKPRRVV
     WAATGKPVLA WESVVEGVQP DGTPSELQVV TDARTGKQLL AAQKVETGTG TGQYVGTVPL
     GTTPSGSTYQ LVDPDRAGHK TYDLNQGTSG TGTLFTDDND AWGDGLPSNR QTAGVDVAFG
     AAATWDYYKD TYGRNGIRND GVAAYSRAHY GSNYVNAFWQ DSCFCMTYGD GSGNTHPLTA
     LDVAAHEMSH GVTAATAGLN YSGESGGLNE ATSDIFAAAV EFYENLPADP GDYLVGEKID
     INGDGTPLRY MDKPSKDGAS HDSWSSTLGS IDVHYSSGPA NHFFYLLSEG SGAKTVNGVS
     YDSPTYDGRP VTGIGIQNAA AIWYRALTTY MTSTTDYAGA RTATLSAAAD LFGAYSPTYL
     AVADAWAAIN VGNRVALGVN LAPVGDQTSG IGQAVSLQVD AYTTNTAASL TYEATGLPDG
     LSISPSGLIT GTPTTLGTSD VTIKVTDSTG ASASKTFTWR IAYVYANAAR VDIPDNGPAV
     ESPVTITGRD GNASATTSVY VNIVHTYRGD LTVDLVGPNG TVYSLLDRSG GSADNVDQAF
     TVDASAQPLN GTWKLRVQDR ASIDVGYIAR WQLTP
//
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