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Database: UniProt
Entry: A0A017RXG9_9CLOT
LinkDB: A0A017RXG9_9CLOT
Original site: A0A017RXG9_9CLOT 
ID   A0A017RXG9_9CLOT        Unreviewed;       521 AA.
AC   A0A017RXG9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=Q428_07075 {ECO:0000313|EMBL:EYE88615.1};
OS   Fervidicella metallireducens AeB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Fervidicella.
OX   NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE88615.1, ECO:0000313|Proteomes:UP000019681};
RN   [1] {ECO:0000313|EMBL:EYE88615.1, ECO:0000313|Proteomes:UP000019681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AeB {ECO:0000313|EMBL:EYE88615.1,
RC   ECO:0000313|Proteomes:UP000019681};
RX   PubMed=24786951;
RA   Patel B.K.;
RT   "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT   Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL   Genome Announc. 2:e00345-14(2014).
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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:EYE88615.1}.
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DR   EMBL; AZQP01000017; EYE88615.1; -; Genomic_DNA.
DR   RefSeq; WP_051515019.1; NZ_AZQP01000017.1.
DR   AlphaFoldDB; A0A017RXG9; -.
DR   STRING; 1403537.Q428_07075; -.
DR   MEROPS; M04.018; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000019681; 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; 3.10.450.490; -; 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   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:UP000019681};
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..26
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           27..521
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023002653"
FT   DOMAIN          67..116
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          220..360
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          365..520
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        444
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   521 AA;  58404 MW;  CE0DDC324AC68176 CRC64;
     MKRFLSVFLT FLVTAFIVCI PVTSSAAKSN HNFLVKNMGK YSKDIKGIAK FFKDYKKEFN
     VEDAEKELVF KNSKNDNLGY THVKLQQVVD GIPVYGKEYI IHYNNKDEVY AVNGNFDVKA
     KQFKRNKEFI KEKDAVAIAI AQVNFDSESL NTDLSDNLVP KLFLYELNEE YIPVYLIRIN
     FLSPVPGDWF IFINALNGEV VEKYNKIRTV SVTGSGIGVL GDTKTLNLDK VTVKIRNKTE
     TQYQTNDLTR SAVITTYTAN NATRLPGSIV YSLSQIINDP AAVDAHYYAG VVYDYYKTKF
     GRNGIDNGNM TIKSTVHYSR NYVNAFWNGS QMVYGDGDGV NSLALSGGLD IIAHEMTHGV
     DEYEADLIYK DQSGALNESF SDCFGTFIEY FAQKNKFDWE MGEDVWTPKI ANDALRSLQD
     PTKYGDPAHM NDYNYTTSDN GGVHTNCGIP NKACYLIATS SGMTIEKTEQ IYYRALVNYL
     TQSSDFKAAK EALIQSAVDL YGVNSVEANA VKAAFEAVGI Y
//
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