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Database: UniProt
Entry: A9WUL5_RENSM
LinkDB: A9WUL5_RENSM
Original site: A9WUL5_RENSM 
ID   A9WUL5_RENSM            Unreviewed;       548 AA.
AC   A9WUL5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   OrderedLocusNames=RSal33209_3168 {ECO:0000313|EMBL:ABY24886.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY24886.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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}.
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DR   EMBL; CP000910; ABY24886.1; -; Genomic_DNA.
DR   RefSeq; WP_012246528.1; NC_010168.1.
DR   AlphaFoldDB; A9WUL5; -.
DR   SMR; A9WUL5; -.
DR   STRING; 288705.RSal33209_3168; -.
DR   KEGG; rsa:RSal33209_3168; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_010362_0_0_11; -.
DR   Proteomes; UP000002007; 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; 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:SF1; BACILLOLYSIN; 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:UP000002007};
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..28
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           29..548
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023023658"
FT   DOMAIN          104..135
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          273..370
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          374..547
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        459
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   548 AA;  56379 MW;  7AD090DD7425B90A CRC64;
     MKKYYAVTGI ALAVGMLCTT QLAGATQAAD PSVGSLDSSN VVTEFSAQGN VEQITFKSAI
     KSAPMSSARS AQTSAIIPGL KNLFVSAPGS DFSLNDSSNN YIKRFTQNIA GIPVLGSSIT
     EVLDGQGAVT SAIGAVTSAT KGAFPADLAA GQAAALASAT KIASAGKDAS AISLVDQKAI
     WFDAVLIGKG ATGSVAVPAY QFSFTTGFAE SRVLTVAAND GAILNDRTDR KDINRVVCDA
     NSKVIDLEAS NADALLKCGK TQANKPTRIE GQAASSVADV NSVYNFLNDT ASFYGANTKA
     NDLTALIGND EGDGLGKAMR AVVRICVTDS QNGEQCPFAN AFWYNGQMTY GQGVTTDDIT
     GHELTHGVTE KTNGLVYANE SGAINESMSD VFGEFIDLSN GSSDDTAANR WAIGEGSSLG
     VIRSMKDPGK YGEPAIYKGS NWKPTATNPN DNNDQGGVHS NSGVGNKLAF LITDGQTFNG
     QTVTGIGIAK AAQLYWAAQR QLTANATYSS LGKALNSACS ANVSNNVAGT TAANCTQVAN
     AIKAVGIK
//
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