ID Q6MHE7_BDEBA Unreviewed; 608 AA.
AC Q6MHE7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=YusX protein {ECO:0000313|EMBL:CAE80980.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:CAE80980.1};
GN Name=yusX {ECO:0000313|EMBL:CAE80980.1};
GN OrderedLocusNames=Bd3602 {ECO:0000313|EMBL:CAE80980.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE80980.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE80980.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; BX842656; CAE80980.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6MHE7; -.
DR STRING; 264462.Bd3602; -.
DR KEGG; bba:Bd3602; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_1_7; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR034006; M3B_PepF_2.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435, ECO:0000313|EMBL:CAE80980.1};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 124..188
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 208..583
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 608 AA; 70297 MW; 9E178958AD96E9C4 CRC64;
MFFCPYGKIF PMEKMAWNLE SEYPSYNSPE FLSEFDLVKS KVDQLEKDVK SLKTPFDNDV
EKIQKIWIDV EATQVLVGNM STFLNCHLSV DSTLSEAQAK KSEVMALSSR MWQILIPVDN
FMKRCSEETL NKILSHPELT PAKFDWSQER TQKPFMLSDD EETLLQALSM PGLHAWGELY
SNLSGTMRCE MKFKDRTETV GLAKASALIR SQDEETRHVA WTSIQEAWTT HKETASAILN
ALSGWRHEVI KKRSQVKPAH YLDQSLFYSR ITKETLDAML TACYENVDMS RRANLAMAKL
MGKKALDPWD LLAQSPISAS KAERSYEEGL KMIKDAFGQA SPEMAQFVDM MAEKHWIEAR
VLPNKRNGAY CTGFRKKREP RVFMTYMGSN SDISTLAHEL GHAYHSWVMR DMPIAECGYP
MTLAETASIF SETLLHDVLL TNAKTREEKI EFAWGEMDRA TAFLLNIPAR YDFEKSFYEM
REKRTVSADE LSKLTDDAWS KWYGSTLSEN DKMYWATKLH FSMSGISFYN YPYTFGYLFS
ISVYARREEL GKDFMQTYIN ILRDTGRMTA EDLVQKHLGE DIRRPEFWRK SIAVINRKIE
EFEKLALG
//
