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Database: UniProt
Entry: A0A0N0HIW6_9ACTN
LinkDB: A0A0N0HIW6_9ACTN
Original site: A0A0N0HIW6_9ACTN 
ID   A0A0N0HIW6_9ACTN        Unreviewed;       529 AA.
AC   A0A0N0HIW6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=ADK82_25605 {ECO:0000313|EMBL:KPC79510.1};
OS   Streptomyces sp. NRRL S-4.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519471 {ECO:0000313|EMBL:KPC79510.1, ECO:0000313|Proteomes:UP000037987};
RN   [1] {ECO:0000313|Proteomes:UP000037987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-4 {ECO:0000313|Proteomes:UP000037987};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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:KPC79510.1}.
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DR   EMBL; LGKJ01000176; KPC79510.1; -; Genomic_DNA.
DR   RefSeq; WP_053930631.1; NZ_LGKJ01000176.1.
DR   AlphaFoldDB; A0A0N0HIW6; -.
DR   STRING; 1519471.ADK82_25605; -.
DR   PATRIC; fig|1519471.3.peg.5374; -.
DR   Proteomes; UP000037987; 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   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..529
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023158861"
FT   DOMAIN          85..130
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          204..350
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          354..528
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        431
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   529 AA;  54458 MW;  4400D8FBD9238A3C CRC64;
     MTPHMNTRRA AALAAVAAMV VVGVQSGTAT AGSNTAGADA SSARTTAGAT TLGVNTAGQR
     GTAIRAAQAD APTAAESLGL GSQEKLIVRD VIKDAHGTVH TRYERTYAGL PVLGGDLVTH
     TAADGKSKGV DKANDARISV PSTQAKVKSA ASARKVVWAG GGKPVLAFES VRTGVRKDGT
     PSRLHIITDA TTGKKLHSFE AVETGTGNSQ YSGEVTLSTT KGSSGFELAD GDRGGHRTYD
     LNQGQTGTGD LVTDADDTWG DGTGGDRQTA AVDAHYGAAK TWDFYKSELG RDGIGGDGKA
     AYSRVHFGTG YVNAFWDDSC FCMTYGDGAD DKSALTAIDV AGHEMTHGLT AATANLDYAG
     ESGGLNEATS DILGSSVEFF ADNTTDAGDY LIGEKIDING DGTPLRYMDK PSKDGGSADY
     WDSGVGDLDV HYSSGVANHF FYLLAEGSGA KTIGGVDYDS PTADGSTVTG IGRQKAYQIW
     YKALSVYMTS STDYAGARVA TEKAATDLFG ADSAELAAVD AAWTGVNVK
//
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