ID A3JVJ2_9RHOB Unreviewed; 612 AA.
AC A3JVJ2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Peptidase M3B, oligoendopeptidase-related clade 3 {ECO:0000313|EMBL:EBA02374.1};
GN ORFNames=RB2150_16412 {ECO:0000313|EMBL:EBA02374.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA02374.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA02374.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02374.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EBA02374.1}.
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DR EMBL; AAXZ01000010; EBA02374.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JVJ2; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09610; 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; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000004731};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 133..202
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 217..597
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 612 AA; 68886 MW; CA1BCDD50C11C6CD CRC64;
MFQFTPRPQF EILRDAATSG GTNEFGDLPE WNLDDLYKGE EASELTRDMA WLENACADFA
KTYEGNLAGL NADAMLECIL AYEKIDSTAG RIMSFAGLRY YQNTTDADRA KFMSDCQENI
TVFTTPLVFF SLEFNRIEDA DYEAIIAANA DLARYRPVLD RMRAMKPYQL SDELEKFLHD
QSTVGSAAWN RLFDESMAGL EFEVDGEMLP LEATLNLMSD QDRATREKGA RAVAAVLQDN
VKLYARIHNT LAKEKEIEDR WRGLPTPQTG RHLSNHVEPE VVEALRNAVV AAYPKLSHRY
YALKAKWMGL DEMQVWDRNA PLPSEIKRTV PWDEAEDLVM KAYGDFAPEM AELAKPFFTD
GWIDAAVKPG KAPGAFAHPT VTDVHPYVML NYLGKPRDVM TLAHELGHGV HQVLAAEQGE
MLSSTPLTLA ETASVFGEML TFRKMLEGAK DQSERKILLA GKVEDMINTV VRQIAFYDFE
CKLHAARADG ELTPDDINAL WMSVQAESLG PVFEYMEGYE TFWAYIPHFV HSPFYVYAYA
FGDGLVNALY AVYEEGTPGF QEKYFDMLKA GGSKHHKELL APFGLDASDP AFWDKGLSMI
SGMIDELEAM ED
//
