ID I4B5T9_TURPD Unreviewed; 453 AA.
AC I4B5T9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:AFM12646.1};
GN OrderedLocusNames=Turpa_1999 {ECO:0000313|EMBL:AFM12646.1};
OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS (Leptospira parva).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Turneriella.
OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM12646.1, ECO:0000313|Proteomes:UP000006048};
RN [1] {ECO:0000313|EMBL:AFM12646.1, ECO:0000313|Proteomes:UP000006048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC {ECO:0000313|Proteomes:UP000006048};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL Submitted (JUN-2012) 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; CP002959; AFM12646.1; -; Genomic_DNA.
DR RefSeq; WP_014803153.1; NC_018020.1.
DR AlphaFoldDB; I4B5T9; -.
DR STRING; 869212.Turpa_1999; -.
DR MEROPS; M16.A15; -.
DR KEGG; tpx:Turpa_1999; -.
DR PATRIC; fig|869212.3.peg.2003; -.
DR HOGENOM; CLU_009902_3_0_12; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000006048; 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:UP000006048}.
FT DOMAIN 22..168
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 177..366
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 453 AA; 51392 MW; F966CB410BD5B8BC CRC64;
MRWISTKPAF QVEKIVLQNG LVVLLENIPH RTSATVGLWL PVGSRFERKR ESGYSHFVEH
MLFKGTRKRH YTEISRAIDR LGGHMNASTS KEITDYYISL SSRHIPVALD VLADMFFDST
FSNEEFVAEK KVIVEELKMG EDQPDDYLFD LFYESQIGDN SLGRPIAGNA RGIQRTTRDE
LYEYYRSHYG PEGTVLSLAG ALYSTPAEKR ALIAEITRHF DRTDHALQGK PGYHREEFRD
AEFQTERAPK QRLLKHQAKD LEQINFVLSL PGEKTQLNQP ADLQVLTHYL GGTMSSRLFV
ELREKKGLCY SVSTFHSQFL HEGVWGIFCA TSPDKYTTAV ETALQEVNEL TTGIDAGDLE
ESKSGLRGSV ELAMESAYRR ASYNARTYLY HGIVKDWRDY LVQLDKVTPT TFLSALRHVW
RGASPGITSL GPKISAATQK KLSNLVKQPL LSQ
//
