ID M8D3M7_9BACL Unreviewed; 533 AA.
AC M8D3M7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=I532_19701 {ECO:0000313|EMBL:EMT50864.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT50864.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT50864.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT50864.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) 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|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:EMT50864.1}.
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DR EMBL; APBN01000011; EMT50864.1; -; Genomic_DNA.
DR RefSeq; WP_003390383.1; NZ_APBN01000011.1.
DR AlphaFoldDB; M8D3M7; -.
DR STRING; 1300222.I532_19701; -.
DR MEROPS; M04.001; -.
DR GeneID; 72736963; -.
DR PATRIC; fig|1300222.3.peg.4139; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000012081; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000012081};
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..32
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 33..533
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023128641"
FT DOMAIN 96..134
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 149..222
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT DOMAIN 230..372
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 375..532
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT COILED 146..176
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 448
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 533 AA; 59434 MW; 64F694EC9034D6A3 CRC64;
MKKSVWKKGF ALTVALSTMT AVPLAHPWSA MAKSSGVQYH EEFETPEFIA EPFEADGLEG
EDLIWSFLES YQKDFQIKGD VQEHFKLLEE VENEETNTRH YRLQEMYNGI PIYGYQQTVH
VDEDGNVTSF LGQFVPNVKE NKKLSRKAKL NEEKALKKAL ADLEDEVGEV EEFEVEPQPE
QYIYVHDGET YLAYAIEFNF LEPEPGRWMY FVDAHTGDII NKYNTIDTVT GTGVGVLGDE
KSFETTRQSS TSYVMRDTTR GSGIETYTAR NATSLPGTLM SDSDNHWTDG AAVDAHAYAQ
RTYDYFRDAH GRNSFDGNGA KIRSTVHYSR NYNNAFWNGS QMVYGDGDGR TFISLSGGLD
VVAHELTHAV TERTAGLIYQ NESGALNESM SDIFGAMVDD DDWQMGEDIY TPGTPGDALR
SLEDPTLYGD PDHYSKRYTG SQDNGGVHIN SGINNKAAYL LAEGGTHYGV TVQGIGRTDT
AKIYYHALTY YLTPYSNFSA MRRAAIQAAT DLFGANSDQV RSVIAAYDAV GVK
//
