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Database: UniProt
Entry: H8G6S9_9PSEU
LinkDB: H8G6S9_9PSEU
Original site: H8G6S9_9PSEU 
ID   H8G6S9_9PSEU            Unreviewed;       451 AA.
AC   H8G6S9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:EHY91312.1};
GN   ORFNames=SacazDRAFT_04475 {ECO:0000313|EMBL:EHY91312.1};
OS   Saccharomonospora azurea NA-128.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY91312.1};
RN   [1] {ECO:0000313|EMBL:EHY91312.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA-128 {ECO:0000313|EMBL:EHY91312.1};
RX   PubMed=22768365; DOI=10.4056/sigs.2635833;
RA   Klenk H.P., Held B., Lucas S., Lapidus A., Copeland A., Hammon N.,
RA   Pitluck S., Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G.,
RA   Land M., Ivanova N., Rohde M., Goker M., Detter J.C., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the soil bacterium Saccharomonospora azurea type strain
RT   (NA-128(T)).";
RL   Stand. Genomic Sci. 6:220-229(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CM001466; EHY91312.1; -; Genomic_DNA.
DR   RefSeq; WP_005445256.1; NZ_CM001466.1.
DR   AlphaFoldDB; H8G6S9; -.
DR   HOGENOM; CLU_009902_3_3_11; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000004705; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          35..182
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          188..367
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   451 AA;  49144 MW;  3C76BAE7EB6198A8 CRC64;
     MARQIAGHLQ KINSTRTLDA GPGVVRRTVL PGGLRVVTES VPGVRSATLG LWVGVGSRDE
     QPKVAGAAHY LEHLLFKGTE RRDATRIAEE IDAVGGEMNA FTSKEHTCFY AQVLDEDLEL
     AVDLVTDVVF AATCEDRDVD TERRVVLEEI AMRDDDPEDL LHETFVETIL PRHPLGRSVL
     GTEQSITDLT PAALRSFYRR RYQPHRMVLA VAGNVEHKDV VRLVRSALGD RLSASDSPTP
     PRSGKARFGR SPGLALHTDE TEQAHLMLGV RALDRHDERR STLSVLNAAL GGGMSSRLFQ
     EVRERRGLAY QVYSSVASYA DAGHLDVYVG CQPDRLGEVA GVVGEVLAEV AENGLTDAEV
     ARAKGQLRGG LVLGLEDTAS RMVRLGKNEL NYGRYESVSD TVARIDAVTA EDVADLARAL
     LRRPRGRAAV AVVGPYAHTD ELPDELHEVM A
//
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