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Database: UniProt
Entry: A0A268JUH2_9BACI
LinkDB: A0A268JUH2_9BACI
Original site: A0A268JUH2_9BACI 
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
//
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