ID D6ZZG0_STAND Unreviewed; 469 AA.
AC D6ZZG0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ADH91155.1};
GN OrderedLocusNames=Snov_3885 {ECO:0000313|EMBL:ADH91155.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Ancylobacter.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH91155.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH91155.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
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; CP002026; ADH91155.1; -; Genomic_DNA.
DR RefSeq; WP_013168656.1; NC_014217.1.
DR AlphaFoldDB; D6ZZG0; -.
DR STRING; 639283.Snov_3885; -.
DR MEROPS; M16.019; -.
DR KEGG; sno:Snov_3885; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_5; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000006633; 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; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 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:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003092338"
FT DOMAIN 42..188
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 195..378
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 443..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 50655 MW; 70569D6971515743 CRC64;
MPALMLIAGA AAGAAGLATA AAPTRAQAAE VSEFTLGNGM QVVVVPDHRA PVVTHMVWYR
VGSADEQPGK SGIAHFLEHL MFKGTDKHPA GEFSQVVAKL GGQENAFTSQ DYTAYFQRVA
KQHLGTVMGF EADRMTGLVL TDEVVLPERD VVLEERRMRT DNDPSAQLSE ASQAAMFVNH
PYGHPIIGWE DEIKKLNRED ALAFYRRFYT PNNAILVVAG DVEPAEVKKL AEETYGKVQP
RAETAARIRP QEPEPRAERR LVLADGRVGQ PSLSRSYLVP SYRTDNKESV ALDVLSQVLG
GGSTGRLYRS LVIEKGLAAS AGAWYQSTAL DETRFGISAM PRPEVTMETM EKALDEAIGA
LATDGPEAGE LERAKTRLVA EAIYAQDNQA TLARIYGATL ATGSTAEDVK NWPEMVKGVT
AEDVREAARR WLLPARAVTS QLLQAKPTPA AALPPAPGAP DGRSPEDRS
//
