ID A0A1Y4GQW7_9BACT Unreviewed; 369 AA.
AC A0A1Y4GQW7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=B5F39_02005 {ECO:0000313|EMBL:OUO94671.1};
OS Cloacibacillus sp. An23.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Cloacibacillus.
OX NCBI_TaxID=1965591 {ECO:0000313|EMBL:OUO94671.1, ECO:0000313|Proteomes:UP000196418};
RN [1] {ECO:0000313|Proteomes:UP000196418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An23 {ECO:0000313|Proteomes:UP000196418};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:OUO94671.1}.
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DR EMBL; NFJQ01000002; OUO94671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4GQW7; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000196418; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000196418};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..369
FT /note="Peptidase M48 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012576530"
FT DOMAIN 61..242
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 369 AA; 40634 MW; 8A4668AD2FE326A7 CRC64;
MAKKILILTL TLALMAAAGA AHAAASPEPS DKTIKREIRI GRKSAEEIEK HVPRVLNPSV
EAKLSMIASR LVPYMQRDLD YEVRILEMKQ PNAFSLPGGM TYITTGMLDF LKSEDEIAAV
LCHEFVHADR AHGIVQARRN SRLNLLTLAG LIAATQAGEG GAGIAAMAGG IQTAMMNSYS
IDLEKEADAM GIDVLYRAGY NPAAMLTMME RMNVERLKRA QYELGIFQTH PEADERVEAA
LKYLREKGID IQRKDVVKML KVTVADEKGR TRLLIDGREL FSAPSGDGAR KLFEGVAKRL
DENLELELAP YDIRVGGEPG SQSLIIGRSI ILREDELLPG MPGLSEIRDG VMEAVNRARR
GNILTDYYE
//
