ID A0A2A8S810_9BACI Unreviewed; 553 AA.
AC A0A2A8S810;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=CN326_17180 {ECO:0000313|EMBL:PEZ03945.1};
OS Bacillus sp. AFS018417.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ03945.1, ECO:0000313|Proteomes:UP000220085};
RN [1] {ECO:0000313|EMBL:PEZ03945.1, ECO:0000313|Proteomes:UP000220085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ03945.1,
RC ECO:0000313|Proteomes:UP000220085};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC 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:PEZ03945.1}.
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DR EMBL; NTTM01000043; PEZ03945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8S810; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000220085; 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; 3.10.450.40; -; 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; IPR025711; PepSY.
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:SF3; NEUTRAL PROTEASE B; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000220085};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, 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..27
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 28..553
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023156403"
FT DOMAIN 84..134
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 153..219
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT DOMAIN 244..387
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 390..552
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 380
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 468
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 553 AA; 59656 MW; 041B481813D254C5 CRC64;
MKKKSLALVL AAGMAVATFG GTSSAFADSK NVLSTKKYNE TVQSPEFVSG NLTSASGKKA
ESVVFDYLNT AKKDYKLGEK SAEESFKVQK IIKDPVGEAT VIRLQQIYEG VPVWGSTQVA
HVGKDGVLKV VSGTVAPDLD KKEKLKNKNK IEGKKAIAIA QKDLGFTPKY EVEPSADLYV
YQNGEETTYA YVVKLNFLDP EPGNYYYFIE ADSGKVLNKY NTIHNATNDN TAPSKPVTGT
STVGTGKGVL GDTKSINTTL SGSSYYLQDN THGATIYTYN GNNRTRLPGT LWADTDNVFN
AKSDAAAVDA HYYAGVTYNY YKNTFNRNSY NDAGAPLKST VHYGKNYNNA FWNGSQMVYG
DGDGSTFIAF SGGIDVVGHE LTHAVTEYSS NLIYQNESGA LNEAFSDIFG TLIEYYDNRN
PDWEVGEDIY TPGQAGDALR SMSDPTKYGD PDHYSKRYTG TSDNGGVHTN SGIINKAAYL
LANGGTHYGV TVNGVGKDKV GAIYYRANTV YLTESATFSQ ARAALVQAAA DLYGANSAEV
AAVKQSYDAV GVK
//
