ID A0A0S8E6L7_9BACT Unreviewed; 597 AA.
AC A0A0S8E6L7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK74_06405 {ECO:0000313|EMBL:KPK43718.1};
OS Nitrospira bacterium SM23_35.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704026 {ECO:0000313|EMBL:KPK43718.1, ECO:0000313|Proteomes:UP000051169};
RN [1] {ECO:0000313|EMBL:KPK43718.1, ECO:0000313|Proteomes:UP000051169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_35 {ECO:0000313|EMBL:KPK43718.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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:KPK43718.1}.
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DR EMBL; LJUG01000108; KPK43718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8E6L7; -.
DR Proteomes; UP000051169; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09610; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 114..171
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 200..577
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 597 AA; 69684 MW; D0FC795DE547B58B CRC64;
MRPSEWNLKL LFRGDDDPRI AKTRKIVEQK SRAFINKWRN RTDYLRNPAV LKKALDEYQE
WKRYYGSEGD EGYYFWLRTS QNQNDPVLRA KFNLIEEFSK KIQNDIQFFT LRIAKIPVRF
QKKFIQHPSL RKYWHYLERL FAQSRYLLSE PEEKIMNLKS PGSYGNWVRM TSSFLAKEER
PVILENGQRS LKSFSEIASL MNSREKRVRN TAAKAFNEIL NKHADVAEAE INAVLANKKV
DDELRCFSRP DSARHISDDM DTEVVDTLIT SVAGGFDIPS RFYSLKARLL RVRTLQYHER
NVEYGTISSK YPYQNALNLI RKVCGNLDHT FVHILDGFIR NGQFDIYPRK GKTGGAFCAH
NLISQPTYIL LNHTNRLNDV LTLAHELGHG INNELIREKQ HSLYFGTPVS TAEVASTFME
DFVLQEIIRK ADDEMRLAVM MMKLNDEVST IFRQIACYRF EQELHERFRK TGYLSKEDIG
QLFQKHMKSY MGNSVEQSPG SENWWVYWGH IRSFFYVYSY ASGLLISKSL QNSVKKDPRF
IGKVKEFLSA GLSDSPKNIF RGLGIDITDK KFWVRGLEEV ETLLNETAHL ATKLGKI
//
