ID B4UX78_9ACTN Unreviewed; 678 AA.
AC B4UX78;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=M444_01835 {ECO:0000313|EMBL:AKL64382.1}, SSAG_00234
GN {ECO:0000313|EMBL:EDX20443.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX20443.1, ECO:0000313|Proteomes:UP000005764};
RN [1] {ECO:0000313|EMBL:EDX20443.1, ECO:0000313|Proteomes:UP000005764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX20443.1,
RC ECO:0000313|Proteomes:UP000005764};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., Straight P.,
RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA Lander E., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. Mg1.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKL64382.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL64382.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
RN [3] {ECO:0000313|EMBL:AKL64382.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL64382.1};
RA Hoefler B.C., Straight P.D.;
RL Submitted (JUN-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}.
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DR EMBL; CP011664; AKL64382.1; -; Genomic_DNA.
DR EMBL; DS570384; EDX20443.1; -; Genomic_DNA.
DR RefSeq; WP_008734766.1; NZ_DS570384.1.
DR AlphaFoldDB; B4UX78; -.
DR STRING; 465541.M444_01835; -.
DR MEROPS; M04.017; -.
DR KEGG; strm:M444_01835; -.
DR PATRIC; fig|465541.12.peg.463; -.
DR eggNOG; COG3227; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_008590_5_1_11; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000005764; Unassembled WGS sequence.
DR Proteomes; UP000035653; Chromosome.
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; 3.10.450.40; -; 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:UP000035653};
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..33
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 34..678
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5014085158"
FT DOMAIN 561..678
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 29..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 369
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 456
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 678 AA; 69739 MW; D9DCA83C80CF2335 CRC64;
MKSTHRRNAT ATSALLTAAA LLTVGVQAGS ASAQPEESNT TASQGRSVPN PGALPAQLSP
SQRAELIAKA QGTTAATAQE LGLSPQEKLL VHDVVKDQDG TTHTRYERTY EGLPVLGGDL
VVNRTAADRT QSVAKASAAE LQGVSVSAPA DAPAAASAKA LDAAKAIGSK ADKAEAAPRK
IVWMAKGVPT LAYETVIGGL QDDGTPNQLH VITDAKTGAK LHQWQGIETG VGNTHYSGQV
TLGTSTSGSN FTLNDAGRGG HKTYNLNRGT SGTGSLFSQS NDTWGNGANS NAATAGADAA
YGAGVTWDFY KNVLGRSGIR GDGVAAYSRV HYGNAYVNAF WDDGCFCMTY GDGTGNNDPL
TSLDVAGHEM THGVTAATAG LEYSDESGGL NEATSDIMGT SVEFYANNPS ARGNYLIGEQ
IDINGDGTPL RYMDKPSKDG GSKDAWYAGI GNLDVHYSSG PANHWFYLAS EGSGAKTVNG
VSYDSPTSDG LPVTGIGRDK AQLIWYKALT TKFNSSTDYA GARAGTIAAA TELYGAGSAE
VKTVTDAWAA VNVGTRSTGT TTPGKVFEST SRVAIPDSPG PAVTSSVTVS GVTGNAPSAL
KVGVKITHTY IGDLQIDLVA PNGTSFRLQN SSSDSKANLD KTYTVNAAAA AANGTWKLKV
QDKGAGDVGT ITDFKLTF
//
