ID A0A0K1EP26_CHOCO Unreviewed; 948 AA.
AC A0A0K1EP26;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=pepN {ECO:0000313|EMBL:AKT42559.1};
GN ORFNames=CMC5_067860 {ECO:0000313|EMBL:AKT42559.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT42559.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT42559.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT42559.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; CP012159; AKT42559.1; -; Genomic_DNA.
DR RefSeq; WP_050434165.1; NZ_CP012159.1.
DR AlphaFoldDB; A0A0K1EP26; -.
DR STRING; 52.CMC5_067860; -.
DR KEGG; ccro:CMC5_067860; -.
DR PATRIC; fig|52.7.peg.7449; -.
DR Proteomes; UP000067626; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..948
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005459750"
FT DOMAIN 61..258
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 300..514
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 597..922
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 27..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 456
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 948 AA; 103113 MW; FDA9D4B111159D89 CRC64;
MTALRRLLCA AAVPLSASLF AACTPREAPA PHAPPAAGSP SIAVVDDGTQ PPLGPLPGDV
KPLDYQLTLQ IDPEKDHFSG TARIIIDLSA PRSTLWMHAR DLRVKSATIQ PDVNGALARA
STCRACVLPP ENQPVFPARF EQVDPTGVAK LSFEQPIPKG WAILVLDYEG PLPEGNSGLY
RVRRGGRAYA FTQFEATSAR QAFPSFDEPA FKTPFHVNLI VPRDHTAISS GAQVNRVREN
DQLDRVTFAT TQRLPTYLLA FAVGPFDVVK APSIPPSIIR HRELPLRGVA VAGRGSELAF
ALANTGSLIQ ALEDYTGLPY PFDKLDLIAV PGKHGAMENA GAVTFSEYLL LMDAVRSPAR
QRRAFFDVGA HEFAHMWFGD LVTMPWWNDL WLKEASANWL GTRAVRMVYP ALDLESEMLS
DVHRAMNTDS LLAARKIRQE IDSHHDISNA FDGITYDKGY GVISMFERWL GPEVYQRAVR
SFFMSRMYGT ASADDYLAAL GQAASRDVAT PMRTFLDQPG VPLVKARLTC EGKPRLRLEQ
SRYLPLGSAG APAAQWQIPI CARYPRGQGA DATETTCTLL DGREGEIQLA SEQCPAWVLP
NADGVGYFRW TLPSADLQRL ITAGLAHLSV REKMSLAANI HAAFAQGTTS GKEALTLLAP
LATDARHEVA TAPIPLLQAA LQWLAGGPSH ARVEAYARAL YAPAYRSLGW GPRAAGPGAT
PQPEPEENSY LRTDVLRFLA LDARDPQVRK EAAARGRAYI AGGTLHPETV APELAGIVVA
AALQQGDAAL FEQALAALAS TEHDVPRGVV LFGLGSIDTP ELATRVRELV FDARVRPHEI
YSILSLQLEQ PAVRDAAWSW FEQKLDAILQ RLSHRHKRGL IHLAASLCDS AYAGRVEALF
TPRIAGLEGG PRVLAGTVET IKLCAARKKA QQESLNAFFE TSPRVPHQ
//
