ID A0A0Q5HCX7_9BURK Unreviewed; 937 AA.
AC A0A0Q5HCX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Zn-dependent peptidase {ECO:0000313|EMBL:KQQ92035.1};
GN ORFNames=ASF77_08940 {ECO:0000313|EMBL:KQQ92035.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ92035.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ92035.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ92035.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ92035.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ92035.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQQ92035.1}.
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DR EMBL; LMOJ01000012; KQQ92035.1; -; Genomic_DNA.
DR RefSeq; WP_056338987.1; NZ_LMOJ01000012.1.
DR AlphaFoldDB; A0A0Q5HCX7; -.
DR STRING; 1736272.ASF77_08940; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
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; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..937
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006251391"
FT DOMAIN 60..215
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 224..399
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 680..857
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 937 AA; 101240 MW; 0F2A60356B8D8685 CRC64;
MKVLVALMVS AGILSPVFAA RAGAPAPAQA KAAIQNDPAK VTSVEGITEY RLANGLRVLL
FPDASKPTLT TNMIYMVGSR HENYGETGMA HLLEHLLFKP TANFGVKKGT KSPVEILNGL
GADFNGTTWY DRTNYYATFP ANEANLNTML ALEADRMINA PISQDDLWNT KTNKGEMTVV
RNEFEIGESN PVRVTLQRLQ AVAYDWHNYG KSTIGARSDI EQVNIPRLRA FYKQYYQPDN
AVLIVAGRFD EAKVLAQVNT LFGKIPKPSR VIQPTYTLEP VQDGERSVVV RRSGGTQYVG
AGYHIAPSGH PDAAALQVLA RVLTDAPSGR LHKALVETKL ATAVNGMSVS NLEPGYRIFG
AVVPKDLPLA PAQETLLKVL EDLKSNPVTE AEVARARQAI SKNIELAMTD SASLTIGLTE
AMAAGDWRLF FVNRDQVEKV DVKAVQAAAE KYLKASNRTL GVFVPTDAAD RTDVPGKIDV
AAVVNDYKGR AVVAQGEVFD PSPANIEART QRFKLANGLQ GALLPKKTKG NLVTATIRLR
FGTEEALRNK ATTGAFTAGL LSYGTQDKSR QQVKDMFDKL KAQPRISGGA EGVTASVTTT
RENLPAAMDL LAEVLRKPAF APTEFGEFQR ANINATEQSI PEPNPQASVA LSRLLDTTPE
GHVKHAMTLQ QRLAAQKAAS VEEVKAFHSA FYGADNATFA AVGDFDPAAL KAQVERLYGD
WKAQQKYVRV PAAVKPVAGQ KLALETPDKA SSLLLAVHPV PLKDDAKAYP ALVMANWMLG
GGALRSRLAD RIRQKEGLSY GVGAQLNVPT RDAAGYWMAY AMSAPQNTAK VETVLREELE
RAVKEGFTDA ELAEAKKGWL QGEEVSRTSD EALAGALSEY LTLDRTMAFD AAVEDQVRKL
TVAQVNEAMR AYIKPSDISF VTAGDFAKAA KGASGVK
//
