ID   C4L1B3_EXISA            Unreviewed;       509 AA.
AC   C4L1B3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   OrderedLocusNames=EAT1b_0125 {ECO:0000313|EMBL:ACQ69059.1};
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ69059.1, ECO:0000313|Proteomes:UP000000716};
RN   [1] {ECO:0000313|EMBL:ACQ69059.1, ECO:0000313|Proteomes:UP000000716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX   PubMed=21460088; DOI=10.1128/JB.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
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}.
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DR   EMBL; CP001615; ACQ69059.1; -; Genomic_DNA.
DR   RefSeq; WP_012726178.1; NC_012673.1.
DR   AlphaFoldDB; C4L1B3; -.
DR   STRING; 360911.EAT1b_0125; -.
DR   MEROPS; M04.001; -.
DR   KEGG; eat:EAT1b_0125; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_008590_5_2_9; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000000716; Chromosome.
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   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   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..22
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           23..509
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023144821"
FT   DOMAIN          51..95
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          120..179
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          199..343
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          346..508
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        424
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   509 AA;  54569 MW;  CF0EE131B64AFC71 CRC64;
     MKKVVSTSLI AGVLLVPQLV GAAELKSGTL TKPSESAPTT IVKEYVKSKG EFKTIESKSD
     KVGKVVKLQQ TVDGVPVFGG VVVGVVDEAG QLKTVVDDAK SVKNLHKSIK LTEKKAIASY
     KKLVGHKGAY ELEPEAELIV YPKGDKSVYA YQVTGTILEA EEPSRWTYFI DAGTGEVLNK
     FDQLAHARPT NGVTGTTYTG TGIDVLGYSQ TFKTTKSGSY YYLQDSTRGK GIYTYDAKNR
     TTLPGSLWAD VDNVLNTTYD RAAVSAHVNA TKTYDFYKNT YGRNSYDNAG AALNSTVHYS
     RSYNNAFWDG SKMVYGDGDG QTFTYLSGAL DVVAHELTHA ITEYTAGLIY QNESGAINEA
     VSDILGTVAE YSVGTNFDWL VGEDIYTPGV AGDGLRSMAN PAAYGDPDHY SKRYTGTQDN
     GGVHINSGIV NKAAYLLGNG GSHYGVSVQG VGVMAMGDIY YRALNVYLTP TSNFSSLRQA
     VVQSAKDLYG ATSPQAVSAA KSFDAVGIY
//