ID H6L2C6_SAPGL Unreviewed; 753 AA.
AC H6L2C6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Zn-dependent aminopeptidase {ECO:0000313|EMBL:AFC24764.1};
GN OrderedLocusNames=SGRA_2033 {ECO:0000313|EMBL:AFC24764.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC24764.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC24764.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC24764.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
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DR EMBL; CP002831; AFC24764.1; -; Genomic_DNA.
DR RefSeq; WP_015692384.1; NC_016940.1.
DR AlphaFoldDB; H6L2C6; -.
DR STRING; 984262.SGRA_2033; -.
DR KEGG; sgn:SGRA_2033; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_015077_0_0_10; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000007519; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:AFC24764.1};
KW Hydrolase {ECO:0000313|EMBL:AFC24764.1};
KW Protease {ECO:0000313|EMBL:AFC24764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007519};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..753
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003603816"
FT DOMAIN 364..561
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 753 AA; 88845 MW; C6AAC0E1420702B0 CRC64;
MLKRSLLAIL GLFLLAQYGW AQEERAHEKF KQLYEELPTP NQYHNAAGAP GHKYWQQRAD
YNIQVRLDDE KQRIYGKERI AYYNNSPDEL SYLWLQLDQN VRAQGSDAQI TETQKLDPQM
YSYQVMSLFD KFDGGFKIEK VSGKKGENLK YTINKTMMRI DLDRPLKPGE KFEFDVKWWY
NINDGIKTRA RSGYEYFPED DNYMYNIAQF YPRMCAYNSV DGWQNKQFMG RGEFTLSFGN
FNLEITVPKN FIVGATGVLQ NSKDVLSKTQ RERIEKARTA KDPVFIITEE EAKANESKKG
EGSQTWRFYA SNVRDVAFVA SRKLIWDAQG VQFGDRNVLA ISYYPKECMG LWDKYSTRAV
VHTLKTYSKY TFDYPYPVAI SSHANFTGME YPMICFNYGR PRPDGTYSER LKYGMIGVII
HEIGHNYFPM IVNSDERQWT WMDEGLNTFL QYLTEVEWER DYPCRRGPAY KITDYMGGDK
NGIVPIMTNS ESILQFGNNA YGKPATALNI LRETIMGREL FDHAFKEYAN RWKFKHPTPA
DFFRTMEDAS GVDLDWFWRG WFYGTDHVDI ALDEITHYHL NTFNPEQEMS MQKIWDAEDP
TYIGDIRNKE SVKQTVMERY PDLRDKYNDR DKYRVDEETQ RNSLFAYQNL SAEEKEVLAK
DYNYYQVDFK NVGGLVMPII IELKYVDGSS EVRYIPAEIW RYNSNKVSKV FVTEKEIKEF
ILDPYLETAD VERENNYFPR RRKPTRFEMF SPR
//