ID A0A0D1CQD3_9RHOB Unreviewed; 467 AA.
AC A0A0D1CQD3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=PepB protein {ECO:0000313|EMBL:KIT16992.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:KIT16992.1};
GN Name=pepB {ECO:0000313|EMBL:KIT16992.1};
GN ORFNames=jaqu_11820 {ECO:0000313|EMBL:KIT16992.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT16992.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT16992.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT16992.1,
RC ECO:0000313|Proteomes:UP000032232};
RA Voget S., Daniel R.;
RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT Roseobacter clade.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:KIT16992.1}.
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DR EMBL; JYFE01000023; KIT16992.1; -; Genomic_DNA.
DR RefSeq; WP_043918030.1; NZ_JYFE01000023.1.
DR AlphaFoldDB; A0A0D1CQD3; -.
DR STRING; 935700.jaqu_11820; -.
DR PATRIC; fig|935700.4.peg.1228; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000032232; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR048816; Peptidase_M17_N_1.
DR PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF21337; Peptidase_M17_N_1; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KIT16992.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIT16992.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000032232}.
FT DOMAIN 311..318
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 467 AA; 50026 MW; 06D05C97C57C95F5 CRC64;
MSAPLFADPD TRAIPLRPVW SDDLEAWLAD QDEPARDWVE ATGFRAKAGE LCRIPGPDLT
VSRVLLGMGR RTTRRRTRFA VARAARALSE GTYRLDGEMT VNDTEEAALG WLLSGYRFTR
YRPGDGGSHP GLIAPRGVDA SRLETIAEGE FLTRDLINTP AQDMGPDELE HAAHDLARRH
QATCTVTTGD DLLNSDLPLI HAVGRASTRA PRLIDLTWGA EDAPKLTLVG KGVCFDTGGL
NLKPASSMGL MKKDMGGAAT VLGLAYMVMA SGLDLRLRVL IPAVENAVAG NAFRPGDVLT
SRSGKTVEIN NTDAEGRLVL ADALTVATED EDARPDLLVC MATLTGAARV ALGPDLAPFY
TDDDALAMAL AHAAARVRDP VWRMPFHRPY ETMIEPGIAD LDNAPSGGFA GSVTAALFLD
RFVPDAVRFA HFDIYGWNPT AAPARPKGGV GQGARALFEA LPKVLAR
//
