ID B0N4H5_9FIRM Unreviewed; 455 AA.
AC B0N4H5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=CLORAM_01526 {ECO:0000313|EMBL:EDS18577.1};
OS Thomasclavelia ramosa DSM 1402.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS18577.1, ECO:0000313|Proteomes:UP000005798};
RN [1] {ECO:0000313|EMBL:EDS18577.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18577.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS18577.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18577.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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:EDS18577.1}.
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DR EMBL; ABFX02000005; EDS18577.1; -; Genomic_DNA.
DR RefSeq; WP_003536964.1; NZ_DS499656.1.
DR AlphaFoldDB; B0N4H5; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_590123_0_0_9; -.
DR Proteomes; UP000005798; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000005798};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 455 AA; 50390 MW; 52BAE1F82BC912E4 CRC64;
MYGKLAWEKY NDEQINDIMT FNEGYKNYIT KGKTERLCVS ETVKLAMAHG YKELNEVDIL
KPGDKVYVTN MKKNIALFVI GKKPLEDGMR ILGAHIDSPR MDLKQNPLYE SEGFAMLDTH
YYGGVKKYQW VTIPLSMVGV VVKKDGTVIN VNIGEDENDP VVGISDLLVH LSADQLKKDG
AKVIEGEDLD VTFGSIPLKD HEKDAVKANV LKILKDKYDF DEEDFLSAEI EIVPSGKARD
YGIDRSMVAG YGHDDRVCAY TSLMAILDIE MPDYTSCCIL VDKEEIGSVG ATGAQSLFFE
NTVSELLLKQ GTDSFVKTRK AMANSKMLSS DVSAGVDPLY LSVNDKKNAA YLGKGIVFNK
YTGARGKSGS NDANPEYMAE IRKILDDDNI YYQTAELGKV DQGGGGTIAY ILGNYNMNVI
DAGVAVLNMH APMEIVSKVD VYEAYLAYRT FLKQI
//