ID A0A4R1L390_9BACT Unreviewed; 963 AA.
AC A0A4R1L390;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:TCK72496.1};
GN ORFNames=C7378_2078 {ECO:0000313|EMBL:TCK72496.1};
OS Acidipila rosea.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=768535 {ECO:0000313|EMBL:TCK72496.1, ECO:0000313|Proteomes:UP000295210};
RN [1] {ECO:0000313|EMBL:TCK72496.1, ECO:0000313|Proteomes:UP000295210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103428 {ECO:0000313|EMBL:TCK72496.1,
RC ECO:0000313|Proteomes:UP000295210};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:TCK72496.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SMGK01000003; TCK72496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R1L390; -.
DR Proteomes; UP000295210; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:TCK72496.1};
KW Protease {ECO:0000313|EMBL:TCK72496.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295210};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..963
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020771773"
FT DOMAIN 65..189
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 225..397
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 532..646
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 685..861
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 963 AA; 104745 MW; D40BE5F48D77A837 CRC64;
MYSKARAFSR SFTLLALAAS ATFVVAQASQ PTPKRPAVHA AEAAQARQLP TIAYQKYTLP
NGLTVLTHED HRLPLVAVDL WYHVGPLNER PGRTGFAHLF EHMMFEGSEH VGEKAHFKDV
QAAGATDVNG TTNFDRTNYF ETMPSNQLEL ALWLESDRMG FLMEGLDRKL LANQRDVVRN
ERRQREGLPY DVADEAVFHL LFPKNHPYYG EVIGSHADIE SARIADVRAF HQQFYTPSNA
SIAVAGDFDP VKLKDLLTRY FGPIPRGPKV EPVHVITPPI TAERRATITD TVQLPRLSVA
WLTPPAFAPD AYSVDAAIFA LGGAKASRLD RSLVIKSQVA QSVTCNTMEL KLTGIASCDI
TAKPGVKLED LEATFWKELA TLQQDGPTAE EVKASKALAL TSKITGLQRL GGFGGVADTL
DRYNQYTGDP DFLPKDVAMT EAVTIASSKA AADKYLSKNS AVVVYCVPGK KILHDVPRSP
DNTDANVKIT NPYTPAFEKS QEWRKNKPTP GPMPTFHLPV PTEFTLNNGL KVLLVQEHAL
PLLTAELVSR AGSDNNKPAT AGLATLVTEV MGDGTESRSL EKLAEDQESI GTHINTNAGM
DYAGISMGVL RSHADEGMDL LADVALHPAF RTADIERRRK QRLVTISQET DNVIQMAMRV
GPKLLFGDQP YGLSGNGTPE TVKAITAEDI SGFYKHRYGP NDSVLVLTGD VSRAEAEKLA
NEYFGKWTSQ AEAAPQIPAA PETPPTHVVI VSKPGAPQTA LFAIGNGVRE NSPDSELLDV
LDYTLGSAFA SRINMNLREV HGYTYGAFSG FKGFRDGGAF FVGSLVRTDV TAPAAKEMMG
EIRNFLVHPS TAEELAAAKE ASIRSLPGRF ETNSAIAYAI QSLFVYDRPL DYYSKLPARY
QDITQADVAR AAKQYLHPDH LIIVTAGDRA KIEPALKAAG LGPVEVRDIS GNVVNTATQP
SGK
//
