ID A0A071LNZ7_9ENTR Unreviewed; 429 AA.
AC A0A071LNZ7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Aminopeptidase B {ECO:0000313|EMBL:KEA50207.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:KEA50207.1};
GN ORFNames=DT73_25395 {ECO:0000313|EMBL:KEA50207.1};
OS Mangrovibacter sp. MFB070.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Mangrovibacter.
OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA50207.1, ECO:0000313|Proteomes:UP000027726};
RN [1] {ECO:0000313|EMBL:KEA50207.1, ECO:0000313|Proteomes:UP000027726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA50207.1,
RC ECO:0000313|Proteomes:UP000027726};
RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT Bacterium Isolated from an Aquaculture Farm.";
RL Submitted (APR-2014) 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:KEA50207.1}.
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DR EMBL; JJMI01000053; KEA50207.1; -; Genomic_DNA.
DR RefSeq; WP_036116354.1; NZ_JJMI01000053.1.
DR AlphaFoldDB; A0A071LNZ7; -.
DR eggNOG; COG0260; Bacteria.
DR Proteomes; UP000027726; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR047620; M17_PepB-like_N.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
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:KEA50207.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KEA50207.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027726}.
FT DOMAIN 276..283
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 429 AA; 46269 MW; 4777078EC1AA5EC6 CRC64;
MTTEVMNITL SSTPADARWG EKALYSINNE GITLHLTGNN DNALIQRAGR KIDGLGFKQV
ALAGEGWDVE KSWAFWMGYR APKGVRNVEW PVLPESEQQE LNNRLKIIDW VRDTINLPAE
DLSPEQLATR AIDLLVDVAG DQVSYRITKG EDLREQNYAG IHTVGRGSAR SPVLLSLDFN
PTGDADAPVY ACLVGKGITF DSGGYSLKQS SFMDSMKSDM GGAALVAGSL AFAITRGLQK
RVKLLLCCAD NMVSGNAFKL GDIIRYRNGK TVEVMNTDAE GRLVLADGLI DASALKPELI
IDCATLTGAA KTALGNDYHA LLSFDDALVS KLMTSATAEN EAFWRLPLAE IHRHQLPSNF
AELNNTAGAV SPAGASTAAG FLSHFVENYQ QGWLHIDCSA TYRKSAVDLW SAGATGIGVR
TLANLLTND
//