ID A7GZS8_CAMC5 Unreviewed; 912 AA.
AC A7GZS8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Zinc-dependent peptidase, M16 family {ECO:0000313|EMBL:ABS50395.1};
GN ORFNames=CCV52592_2215 {ECO:0000313|EMBL:ABS50395.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:ABS50395.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP000767; ABS50395.1; -; Genomic_DNA.
DR RefSeq; WP_011992578.1; NC_009715.2.
DR AlphaFoldDB; A7GZS8; -.
DR STRING; 360105.CCV52592_2215; -.
DR KEGG; ccv:CCV52592_2215; -.
DR HOGENOM; CLU_008156_0_0_7; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000006380; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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; 3.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006380}.
FT DOMAIN 38..176
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 195..372
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 685..842
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 912 AA; 103939 MW; 79779188615B3B1A CRC64;
MRKILLFLVA CIGLFALEQD ADILSGRLEN GLSYYIKENK LPAKTAYFYL IVDSGSTDEA
TNERGLAHFV EHMAFNGSRD FSKNELIKKL EALGVSFGAD LNAQTAYDRT MYKLTIAVNE
NNLKDVFKVY NNWMDGVSFS PEELQKERGV IIEEERQRNT PEYRLFERQA KDLFKDSAYL
DKAPIGDMNI IKSVDALRIK AFYHKLYQPR FMKFVAVGDF DKREIERLIR QNLSEAKNTN
SYSHPDKSIP FRQGLGVYNY DSNETGMNAI RISYFDKHLA RVDEVSARRI LVDSYITSLL
GMLYEQKIAA QNSILRTGFG RPNLQNQQTM YSFETKVTSD DYDAALSDML SVIKGVERYG
FNKEDFNDLK KAFIKSIETR FAQSKTKKSQ TYADEIIAAL ESGSVILSEE ESKNLSLKLL
NEIGLDEVNA EFRRILNLPD KRVSVFSSKG YRLDEAKFKA YENNVTAYDG HTKDQKIATS
LIDDNIAPKA IISKKYDEKH KFYIYTLENN ATVILKPLNT RKDVISFAAI SRGGTSNLAR
PKQGGFATQL SNQSGAGEFN NYQIAKILSD KRISYQKNID MLTQGYYGGS TPEDLKFLFQ
AINLEFNSPR SDPKILEQIK TKTLDNLEKQ KNLPGYKFST EFVRFFYDNN PRMKPLEPSD
VTPLEAGELG KIVQDKFTNA ASYLFVLVGD LDVQKVEPLL QKYIATLPSR PNVENFIDDG
VRSIDGRHKF ERNYETSERS DVMINMINKS APYSKENAIK AKALAEILKM ALREKVREEN
GETYGFALAI TLSKEPYQHS SANISFTCSP KNVDKILSEV KTIENEIKKG GVIDAKHLEN
FKKSAVINIE KSYDQPDFWL RDIIANQIFG EKLFDLDEYK KLINSITNED IKAAAKIYLD
DKNEVISVNN PK
//
