ID X4ZL03_9BACL Unreviewed; 410 AA.
AC X4ZL03;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Peptidase M29 aminopeptidase II {ECO:0000313|EMBL:AHV97350.1};
GN ORFNames=PSAB_12130 {ECO:0000313|EMBL:AHV97350.1};
OS Paenibacillus sabinae T27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV97350.1, ECO:0000313|Proteomes:UP000019772};
RN [1] {ECO:0000313|EMBL:AHV97350.1, ECO:0000313|Proteomes:UP000019772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T27 {ECO:0000313|EMBL:AHV97350.1,
RC ECO:0000313|Proteomes:UP000019772};
RX PubMed=24651173;
RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA Chen X., Cheng Q., Chen S., Li J.;
RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT Genes.";
RL PLoS Genet. 10:E1004231-E1004231(2014).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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DR EMBL; CP004078; AHV97350.1; -; Genomic_DNA.
DR RefSeq; WP_025334869.1; NZ_CP004078.1.
DR AlphaFoldDB; X4ZL03; -.
DR STRING; 1268072.PSAB_12130; -.
DR MEROPS; M29.002; -.
DR KEGG; psab:PSAB_12130; -.
DR PATRIC; fig|1268072.3.peg.2522; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_054346_1_0_9; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000019772; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:AHV97350.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
SQ SEQUENCE 410 AA; 44951 MW; 3B1C73A7A036E928 CRC64;
MTDFEAKLSK YADLAIKIGV NVQPGQALVV NAPIVAAEFV RLIAAKAYEA GASQVKVNWS
DERITRLMFE HAAPEVFTKA PTWYAGEITE FAENGAAVLS VIAEDPDALK GIEQARIANY
HKTRGAALTK YREYVMSDKI SWSIVAIPSQ AWADKVFPDV PAEERIDKLW EAIFHTVRLD
QEEPVAAWQD HLNTLEAKAA VLNAKKYKKL RYAAPGTDLT IELPEGHLWA QGDSINAQGH
TFVANMPTEE VFTAPLKTGV NGTVRSTKPL SYGGNIIDGF SLTFENGKIV SVTAEKGQET
LEHLISLDEG AKYLGEVALV PYHSPISESN ILYYNTLFDE NASNHLAIGT AYAFCLEGGK
SMTQEELEKR GLNTSVTHVD FMIGSAEMNI YGVTGDGTEE PVFLNGNWAF
//
