ID A0A1E5PBQ1_9ACTN Unreviewed; 350 AA.
AC A0A1E5PBQ1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=AS594_23205 {ECO:0000313|EMBL:OEJ26959.1};
OS Streptomyces agglomeratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ26959.1, ECO:0000313|Proteomes:UP000095759};
RN [1] {ECO:0000313|EMBL:OEJ26959.1, ECO:0000313|Proteomes:UP000095759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ26959.1,
RC ECO:0000313|Proteomes:UP000095759};
RA Chen X.;
RT "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL Submitted (AUG-2016) 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:OEJ26959.1}.
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; MEHJ01000001; OEJ26959.1; -; Genomic_DNA.
DR RefSeq; WP_069928831.1; NZ_MEHN01000001.1.
DR AlphaFoldDB; A0A1E5PBQ1; -.
DR STRING; 285458.BGM19_13905; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000095759; 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; 1.10.390.10; Neutral Protease Domain 2; 1.
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; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 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|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000095759};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 93..176
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 179..347
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 270
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 350 AA; 37501 MW; 523619AB76C2B5B1 CRC64;
MKATHPVFCT IVPPHVLDKL AQADDPVLAG PARRTLEADA AQRTHRRLTT VLGARPAASA
TADGKPHRTV HDAQHRQVLP GVKVRGEGEE PGQDATVNRA YAGLGATFEL LLKGFARDSV
DGNGLPLVAS VHYGENYGNA FWDGEQMVFG DGDEIFRDFT LPVDVIAHEL AHGLTQYTAN
LTYFGQPGAL NESVSDVFGS LVKQYVNDQT ADRADWLIGA GLLTDRVTGV ALRSMKAPGT
AYDDDVLGKD PQPAKMEDYV RTGRDNGGVH INSGIPNHAF YLLATDLGGK AWERAGRIWY
DTLTGGSLEV DASFADFARA TVAAARARFG DGEEHEALLK AWSLVGVPTG
//
