GenomeNet

Database: UniProt
Entry: A0A0F2TFT3_STRR3
LinkDB: A0A0F2TFT3_STRR3
Original site: A0A0F2TFT3_STRR3 
ID   A0A0F2TFT3_STRR3        Unreviewed;       542 AA.
AC   A0A0F2TFT3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=VM95_11245 {ECO:0000313|EMBL:KJS62083.1};
OS   Streptomyces rubellomurinus (strain ATCC 31215).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS62083.1, ECO:0000313|Proteomes:UP000033699};
RN   [1] {ECO:0000313|EMBL:KJS62083.1, ECO:0000313|Proteomes:UP000033699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS62083.1,
RC   ECO:0000313|Proteomes:UP000033699};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU366073};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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:KJS62083.1}.
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; JZKH01000017; KJS62083.1; -; Genomic_DNA.
DR   RefSeq; WP_045694872.1; NZ_JZKH01000017.1.
DR   AlphaFoldDB; A0A0F2TFT3; -.
DR   MEROPS; M04.017; -.
DR   PATRIC; fig|359131.3.peg.2051; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000033699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
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; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
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; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033699};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           32..542
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023155382"
FT   DOMAIN          66..113
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          218..364
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          367..541
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          234..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        444
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   542 AA;  56112 MW;  30F899606E85F899 CRC64;
     MKRKLTAGAV LSATALLAGV IQIAAVPAAQ AAAPGPELQQ TSPLSLAAGQ SAPLAQALGL
     PGQERLVAKD AVVDRDGTRH LRYERTYEGL PVLGGDLVVH QRTDGSVASV DRAFDGRLAL
     PTLTPGLAAN QAGEKATAAV RATVGLAADE DEAALARVDG ADAAELVVWA ADGNPRLAHR
     TVVRGERADG TPSRQQVVTD ATSGELLSTH EEIQTASGTG KGVNVGTVPL TTTQSGSTYS
     LKDASRGGQS TTDLKGATSG SGSLFTSTSN SWGNGLVSNR QSAAVDAQFG AAATWDFYKN
     TFGRNGIKNN GVGAASRVHY GSAYVNAFWD DSCFCMTYGD GAGNTHPLTA IDVSGHEMSH
     GVTSATAGLN YSGESGGLNE ATSDIFGTMV EWYANLPANP PNYLIGEKIN IFGNGKPLRY
     MDKPSQDGKS ADSWYSGVGN LDVHYSSGVA NHFFYLLSEG SGAKTINGYT YNSPTSNGAK
     VTGIGRDKAA KVWYRALTVY FTSTTNYKAA RTGTLKAAAD LYGATSAEYK AVAAAWSGVN
     VN
//
DBGET integrated database retrieval system