ID A0A1Q5KPE0_9ACTN Unreviewed; 549 AA.
AC A0A1Q5KPE0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=AMK32_17535 {ECO:0000313|EMBL:OKJ83438.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ83438.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ83438.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ83438.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ83438.1}.
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DR EMBL; LIWA01000003; OKJ83438.1; -; Genomic_DNA.
DR RefSeq; WP_073893734.1; NZ_LIWA01000003.1.
DR AlphaFoldDB; A0A1Q5KPE0; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000186398; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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:UP000186398};
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..37
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 38..549
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023037437"
FT DOMAIN 70..112
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 212..370
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 373..548
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 363
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 451
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 549 AA; 57783 MW; EB1FE0F60878A6C1 CRC64;
MSRIRQHVRG TRRLATTGVA VGTAALMVTA LAPAAHADGR PTRATAIQNA ASALLAHAAG
LGLTSAEDTS VRDVIVDKDG TQHVRYDRTY HRLPVLGGDF VVHLTADGGY RSADRATRGR
ISLASVVPKI SGRKAADLAV NALRAANLGE KLRQVKAKPQ LVVDALHGAP RLAWRTDAAG
LDSLGNPVGR TVLTDARTGA RIDAWDTIET ATGDGKSLYG GTVALETTQS GSAYQLKDPT
RGNTYTGDAA NKTDLCIFGI CFSRAPATLF TDADNHWGTG TTADRSSAAV DAQYGTNETW
DYYKNVHGRN GIAGDGKGSY NRVHYGNNYN NAFWDDSCFC MTYGDGDGTT FGPLVALDVA
GHEMTHGVTS KSAALTYSGE SGGLNEATSD ILGTMVEWYA NNSSDTGDYL IGEKIVRSGF
GKTALRYMDK PSKDGNSADY WSSSVGNLDV HYSSGVANHF AYLLAEGSGA KTINGVSYDS
PTANGSTVTG IGRDKVGKIW YRALTVYMTS STNYAGARTA TLNAAKDLYG AGSAEYNAVA
AAWSAVNVN
//
