ID W2F1C9_9ACTN Unreviewed; 427 AA.
AC W2F1C9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MPTA5024_02090 {ECO:0000313|EMBL:ETK37744.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK37744.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK37744.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK37744.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:ETK37744.1}.
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DR EMBL; AWEV01000020; ETK37744.1; -; Genomic_DNA.
DR AlphaFoldDB; W2F1C9; -.
DR STRING; 316330.MPTA5024_02090; -.
DR PATRIC; fig|316330.3.peg.406; -.
DR HOGENOM; CLU_009902_1_1_11; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 29..143
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 182..360
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 427 AA; 45602 MW; E43D59FE615792C2 CRC64;
MTMPDTASRV RLDCATRRLA NGMLVIVCPD PAQSVAAVHL RYLVGSKHER PGRTGLAHLF
EHLMFTGSPG AADGEHARLI QQAGGFANAA TSMDSTSYFE TVPSGALELV LWLEADRLAG
LPDALDQRIL DVQRDVVKNE RRQTMDTVPY GTALELLVAA LFPAGHPYHH LPIGSMADLD
SASLDDARAF FETFYSPDRA VLTVVGQVEA ETTFAWAERY FGGISRRGQA PLLVTAPRIP
DGDEIRMTMT SDAPPKVFLA HRLPPAGTTA LDAAVLAAAV LARGTAGVLS RGLVRGRALA
AETTFDVVPL AGDASLGVVR LTPRGGTGPS VLERACQAEL ETLAETGVCQ RDLDRAIAQL
EAGWLSRLDL GRGKAEELSW HAMLTGSPES ASEVMARIRA VPAREVADAI SALADRSRRV
VLTYQPA
//
