ID C3MHL0_SINFN Unreviewed; 432 AA.
AC C3MHL0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Peptidase, family M16 protein {ECO:0000313|EMBL:ACP24338.1};
GN OrderedLocusNames=NGR_c05420 {ECO:0000313|EMBL:ACP24338.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24338.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP24338.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24338.1; -; Genomic_DNA.
DR RefSeq; WP_012707123.1; NC_012587.1.
DR RefSeq; YP_002825091.1; NC_012587.1.
DR AlphaFoldDB; C3MHL0; -.
DR STRING; 394.NGR_c05420; -.
DR MEROPS; M16.A15; -.
DR KEGG; rhi:NGR_c05420; -.
DR PATRIC; fig|394.7.peg.3356; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_0_5; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000001054; Chromosome.
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:InterPro.
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:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 15..161
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..340
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 432 AA; 47807 MW; 7373A81C5F24C954 CRC64;
MMKVECTRLP SGLTVVTERM PHLESVALGV WIKSGSRNET VDEHGIAHLL EHMAFKGTRR
RSARQIAEEI ENVGGEVNAA TSTETTSYYA RVLKDHVPLA IDILADILTE STFDEEELRR
EKHVILQEIG AADDTPDDVV FDRFAETAYR DQTVGRPILG TPETVMSFTP GQIRQYLGRN
YTTDRMFIVA AGAVDHDSIV RQVQERFSSL PVAPLSPPVL DTARYTGGDS RESRDLMDAQ
VLLGFEGRAY HARDFYCSQI LANILGGGMS SRLFQEVREH RGLCYSVYAF HWGFSDTGIF
GIHAATGGEN LPELMPVIID ELRKSSTSID QQEIERARAQ IRAQLLMGQE SPAARAGQIA
RQMMLYGRPI PNEELMERLS GITIERLTDL AGRLFFDTAP TLSAIGPLDQ LAPMSDILSS
LNTKSAVHAL AG
//
