ID I7HF97_9HELI Unreviewed; 431 AA.
AC I7HF97;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative zinc protease {ECO:0000313|EMBL:BAM32449.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:BAM32449.1};
GN ORFNames=HCBAA847_1215 {ECO:0000313|EMBL:BAM32449.1};
OS Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM32449.1, ECO:0000313|Proteomes:UP000006036};
RN [1] {ECO:0000313|EMBL:BAM32449.1, ECO:0000313|Proteomes:UP000006036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM32449.1,
RC ECO:0000313|Proteomes:UP000006036};
RX PubMed=23012276; DOI=10.1128/JB.01347-12;
RA Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT BAA-847.";
RL J. Bacteriol. 194:5692-5692(2012).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; AP012492; BAM32449.1; -; Genomic_DNA.
DR RefSeq; WP_015453534.1; NZ_DS990392.1.
DR AlphaFoldDB; I7HF97; -.
DR KEGG; hcb:HCBAA847_1215; -.
DR PATRIC; fig|1206745.3.peg.1275; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_7; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000006036; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 2.
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; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:BAM32449.1};
KW Protease {ECO:0000313|EMBL:BAM32449.1}.
FT DOMAIN 45..146
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 188..362
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 431 AA; 48787 MW; 42777D89EF08B3CA CRC64;
MSVVTSINSA FSTQSVLPKH YTKMLENGLE IVVVPLHNQS GVIETNVFYK VGSRNESMGK
SGIAHMLEHL SFKSTKNLRA GEFDEIVKGF GGVNNASTSF DYTRYFIKSS AENMDKSLEL
FAELMSNLAL EDSEFQPERN VVAEERLWRT DNSPMGYLYF RFFNTAYVYH PYHWTPIGFM
EDIKAWKIED IRAFYETYYQ PQNAIVLVSG DIEPNVVFES ATKHFGALKN RTDSIPQVVA
KEPKQDGERR VIVKKDSQVE YLTMGYKIPN YLSKDQVALS AIGEILSSGK SSIFQTELID
RQQIATSAYA YNMDLKDESV FLIVAAARQG VSAESVEKEI YTILDRLKKG EISQEELEKV
KINTRASFIY SLESAGDVAG LFGSYLVRGD ISPLLRYERE INTLSIEKIK EVANTYFTQD
SLSVVILKDT K
//
