ID D1BGD5_SANKS Unreviewed; 424 AA.
AC D1BGD5;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN OrderedLocusNames=Sked_37690 {ECO:0000313|EMBL:ACZ23652.1};
OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ23652.1, ECO:0000313|Proteomes:UP000000322};
RN [1] {ECO:0000313|EMBL:ACZ23652.1, ECO:0000313|Proteomes:UP000000322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC {ECO:0000313|Proteomes:UP000000322};
RX PubMed=21304646;
RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL Stand. Genomic Sci. 1:110-118(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; CP001819; ACZ23652.1; -; Genomic_DNA.
DR RefSeq; WP_012868720.1; NC_013521.1.
DR AlphaFoldDB; D1BGD5; -.
DR STRING; 446469.Sked_37690; -.
DR KEGG; ske:Sked_37690; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000000322; 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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 424 AA; 44202 MW; 157D2CEF2FCF2287 CRC64;
MQTASDYVAD LARFISASPS SYHTAAEAAR QLDDAGFARL DEAAEWSTPT QRGYVVRDGA
IIAWVAPATA GPTTPFRVLG AHTDSPGFKL KPKPTTGSHG WLQAGVEVYG GPLLNSWLDR
ELELAGRLVT TDGREVLVRT GPFLRIPQLA IHLDREANSG LTLDRQRHTA PVYGVGDRSQ
ADLLGHLAGL AGLSGDDVAG YDVLTADTAA PARFGLDDAL FAAGRMDNLT SVFAGLHALL
GAASEPSPDH VSVLAAFDHE ELGSETRSGA SGPFLDDVLT RVGATLGASA SQRLQAYAGS
WCLSADAGHS VHPNYPEKHD PTNQPVAGRG PLLKINANQR YATDAHGAAL WAGACAAAGV
PYQEFVSNNT VPCGSTIGPL TATRLGIRTV DVGVPLLSMH SARELAHVDD LHGLAAAVGA
FFAG
//
