ID A0A101QSQ2_9ACTN Unreviewed; 679 AA.
AC A0A101QSQ2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=AQJ30_25985 {ECO:0000313|EMBL:KUN35252.1};
OS Streptomyces longwoodensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN35252.1, ECO:0000313|Proteomes:UP000053271};
RN [1] {ECO:0000313|EMBL:KUN35252.1, ECO:0000313|Proteomes:UP000053271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN35252.1,
RC ECO:0000313|Proteomes:UP000053271};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT for the species Streptomyces longwoodensis.";
RL Submitted (OCT-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:KUN35252.1}.
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; LMWS01000033; KUN35252.1; -; Genomic_DNA.
DR RefSeq; WP_067238740.1; NZ_KQ948559.1.
DR AlphaFoldDB; A0A101QSQ2; -.
DR STRING; 68231.AQJ30_25985; -.
DR Proteomes; UP000053271; 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:UP000053271};
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..41
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 42..679
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023160020"
FT DOMAIN 553..679
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
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 679 AA; 70026 MW; 9B98D8A16CD4FE0D CRC64;
MSSRSSRRRT SPTPYRRTAA AALVGVAALV AAAVQSGAAS AAPSSAAAAA RPGAESVRLA
PAQRAELIRQ ADAAKATTAR ELGLGAQEAL VVRDVVKDAD GTVHTRYERT YAGLPVLGGD
LVVDTAKSGD TRGVVKATRA TIKVASLTPA VPADQARKQA LRLAADAGAD SADARRAPRK
VVWAADGTPV LAYETVVGGL QEDGTPNELH VVTDAATGKK LFAYQGIETG TGNTMYSGTV
TLGTSQSGST YTLTDTARGN HKTYNLNRGT SGTGTLFSGP DDVWGNGSAS NAETAGADAH
YGAALTWDYY KNVHGRSGIR GDGVGAYSRV HYGNNYVNAF WSDSCFCMTY GDGSGNTHPL
TAIDVAGHEM THGVTSNTAG LNYSGESGGL NEATSDIFGT SVEFYANNAS DVGDYLIGEE
IDINGNGTPL RYMDKPSKDG ASKDSWYSGI GSVDVHYSSG PANHFFYLLS EGSGAKVING
VSYNSPTSDG LPVTGIGRAK AEKIWFRALS TKFTSTTNYA GARTGTLAAA GELYGTSSAE
YKAVQDAWAA VAVGARSGGG GGGGTTFENT ADVSIPDNGA AVTSSITVSG RTGNAPSNLQ
VAVDIVHTWR GDLVVDLVAP DGTAYRLKSF SSSDSADNVQ ATYTVDASSE VANGTWALRV
QDQAAQDTGY INSWSLTFP
//
