ID A0A0D5AHK6_9NOCA Unreviewed; 350 AA.
AC A0A0D5AHK6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=NY08_4334 {ECO:0000313|EMBL:AJW42336.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW42336.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW42336.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW42336.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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; CP010797; AJW42336.1; -; Genomic_DNA.
DR RefSeq; WP_045198494.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5AHK6; -.
DR STRING; 1564114.NY08_4334; -.
DR MEROPS; M04.025; -.
DR KEGG; rhb:NY08_4334; -.
DR PATRIC; fig|1564114.4.peg.4277; -.
DR HOGENOM; CLU_008590_0_1_11; -.
DR Proteomes; UP000032410; 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; 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; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 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|RuleBase:RU366073,
KW ECO:0000313|EMBL:AJW42336.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 80..162
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 167..334
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 59..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 350 AA; 36949 MW; B3EFF5D5274ABB4C CRC64;
MTFHSVVPPF LLERLQGPGA RATLLADREM RAGREVVQAR TAIAPRTGGT LERTISDAQS
TRDLPGRQVR AEGEDPTGDA ATDEAYDGLG ATYAFFDEVY GYSSLDGSGL PLDATVHYGQ
DYDNAFWDGS RMVFGDGDGE VFARFTVSLG VIAHELAHGF TQYTTPLEYK DQAGALNESI
SDVFGALVEQ YTAGQNAEDA SWLIGEGLFL PAVQGQALRS LLEPGTAYDD DVLGKDPQPA
SMDDFVVTTE DDGGVHINSG IPNRAFAVAA TTLGGPAWDR IGQVWFDTMT VGGLSPTVDF
AGFSAATLAA ATKRFGAGSD VAEAVATGWS TVGVKTTGLE SLPKPSDDRV
//
