ID A0A268JUH2_9BACI Unreviewed; 556 AA.
AC A0A268JUH2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=CHI06_19175 {ECO:0000313|EMBL:PAE38029.1};
OS Bacillus sp. 7884-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021693 {ECO:0000313|EMBL:PAE38029.1, ECO:0000313|Proteomes:UP000216214};
RN [1] {ECO:0000313|EMBL:PAE38029.1, ECO:0000313|Proteomes:UP000216214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7884-1 {ECO:0000313|EMBL:PAE38029.1,
RC ECO:0000313|Proteomes:UP000216214};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-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:PAE38029.1}.
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DR EMBL; NPDD01000167; PAE38029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268JUH2; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000216214; 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; 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; 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:UP000216214};
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..22
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 23..556
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5039752070"
FT DOMAIN 84..132
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 247..390
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 393..555
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 222..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 471
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 556 AA; 59568 MW; A5E25540EE1750E5 CRC64;
MNKKVLALGL SFGLAASTLA AASTYAAPKN VLSNYKYNES VDSPEFVSGE LTKPSAKSPE
SIVHAYVNEN KDKFKLGSKT SEASFIIQSS KKDKFGSTAL RLQQVYNGVP VWGSTQAALV
ADDGVLTVFS GTVAPNLESK KGLKEEKKVN ANKSIKIAEA DLGYTPDYEK NPTSDLVVYT
NGDEATYAYL VNLNFLSPKP GNYNYFIEAS TGNILNSYND LDEAHGQTTS DEGKPSGGSI
TGSNVSGTGK GVLGDSKLLN MTLSGSTYYL QDNTRGGGIF TYDAANRTRL SGSLWTSIDN
LLNSTYDAAA VDAHYYAGKT YDYYKNVFDR NSYDDNGAVV KSSVHYGSNY NNAFWNGRQM
VYGDGDGSNF IPLSGGVDVV GHELTHAVTD STSNLIYQNQ SGALNEAISD IFGTLVEFYD
NNNPDYEIGE DIYTPSIAND AFRSMSDPAK YGDPDHYSKL YTGKADNGGV HINSGIINKA
AYLLAKGGTH YGVTVTGIGN DKLGDIYYRA NTVYLTKSST FSQARAALAQ AAADLYGATS
NEVTSVNKSF DAVGVK
//