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Database: UniProt
Entry: A0A1D2I6A8_9ACTN
LinkDB: A0A1D2I6A8_9ACTN
Original site: A0A1D2I6A8_9ACTN 
ID   A0A1D2I6A8_9ACTN        Unreviewed;       684 AA.
AC   A0A1D2I6A8;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=APS67_005829 {ECO:0000313|EMBL:ODA70032.1};
OS   Streptomyces sp. AVP053U2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA70032.1, ECO:0000313|Proteomes:UP000054731};
RN   [1] {ECO:0000313|EMBL:ODA70032.1, ECO:0000313|Proteomes:UP000054731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA70032.1,
RC   ECO:0000313|Proteomes:UP000054731};
RA   Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL   Submitted (JUN-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:ODA70032.1}.
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DR   EMBL; LMTQ02000047; ODA70032.1; -; Genomic_DNA.
DR   RefSeq; WP_042175924.1; NZ_LMTQ02000047.1.
DR   AlphaFoldDB; A0A1D2I6A8; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000054731; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; PF01483; P_proprotein; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
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, 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:UP000054731};
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..45
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           46..684
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023144555"
FT   DOMAIN          558..684
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        461
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   684 AA;  71421 MW;  9F0E744916278AC5 CRC64;
     MRRRSSHRRT PHAGPRPTHR RTAAVALAGV AALVATAVQA GSATAAPDAT PAARPKPAAE
     SVPLTPAQRA ELIREANATK ADTAEDLGLG TKEKLVVRDV LKDRDGTVHV RYERTYDGLP
     VLGGDLVAQG ERPGAAESVV KATRAAVEPA TTTATVSTAE AKQQALSAAK AEDAKSPDVD
     RAPRKVVWAA SGTPTVAYET VVGGLQHDGT PQELHVVTDA TTGEKLYEWQ AIQNATGHTV
     YSGTVELTST QSGAAYNLTD GARGGHRTYN LNRGTSGTGT LFSGSDDVWG NGSPSNLESA
     AADAHYGAAL TWDYYKNVHG RSGIRGDGVG AYSRVHYGNN YVNAFWSDSC FCMTYGDGSG
     NVNPLTSIDV AAHEMTHGLT SNTAGLIYSG ESGGLNEATS DIFGATVEFH AANSSDVGDY
     LIGEEIDING DGTPLRYMDR PSRDGASKDA WYSGIGSIDV HYSSGPANHF FYLLSEGSGT
     KTINGVSYDS PTSDGLPVTG IGRAKAEKIW FRALTTKFTS TTNYAGARTG TLAATGELYG
     TDSAEYKAVQ DAWAGINVGA RSGDGGGGGT TFENTTDVSI PDNGAAVTSS VTVTGQAGNA
     PSNLRVPVDI VHTWRGDLVV DLLAPDGTAY RLKSRSSGDS ADNVNETYTV NASSETANGT
     WQLRVQDQAA RDTGHINSWG LTFP
//
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