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
//