ID Q4KBR8_PSEF5 Unreviewed; 482 AA.
AC Q4KBR8;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Extracellular alkaline metalloprotease AprA {ECO:0000313|EMBL:AAY92479.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:AAY92479.1};
GN Name=aprA {ECO:0000313|EMBL:AAY92479.1};
GN OrderedLocusNames=PFL_3210 {ECO:0000313|EMBL:AAY92479.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY92479.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY92479.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001205-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001205-2};
CC -!- SIMILARITY: Belongs to the peptidase M10B family.
CC {ECO:0000256|ARBA:ARBA00009490}.
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DR EMBL; CP000076; AAY92479.1; -; Genomic_DNA.
DR RefSeq; WP_011061494.1; NC_004129.6.
DR AlphaFoldDB; Q4KBR8; -.
DR STRING; 220664.PFL_3210; -.
DR MEROPS; M10.060; -.
DR GeneID; 57476230; -.
DR KEGG; pfl:PFL_3210; -.
DR PATRIC; fig|220664.5.peg.3275; -.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_025059_1_1_6; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR016294; Pept_M10B.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR NCBIfam; NF035945; Zn_serralysin; 1.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR Pfam; PF13583; Reprolysin_4; 1.
DR PIRSF; PIRSF001205; Peptidase_M10B; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|EMBL:AAY92479.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001205-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:AAY92479.1}; Protease {ECO:0000313|EMBL:AAY92479.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001205-2}.
FT DOMAIN 71..242
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-1"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
SQ SEQUENCE 482 AA; 49840 MW; 9F74A74750F881B0 CRC64;
MSKVTENAIA SAEQQLVPLA AASSAYNQIN SFSHQYDRGG NLTVNGKPSF SVDQAATQLL
RDGAAYKDLN GNGKIDLTYT FLTSASSSTM YKHGISGFSQ FSAQQKAQAV LAMQSWADVA
NVVFTEKASG GDAHMTFGNY SGGQDGAAAF AYLPGTGAGY DGTSWYLINS SYTQNKNPDL
NNYGRQTLTH EIGHTLGLAH PGDYNAGEGN PSYKDASYGQ DTRGYSVMSY WSESNTSQNF
SKGGVEAYSS GPLMDDIAAI QKLYGANYST RAGDTTYGFN SNTGRDFYSA SSSSDKLVFS
VWDGGGNDTL DFSGFTQNQK INLNEASFSD VGGMVGNVSI AQGVTVENAI GGSGNDLLIG
NNAANVLKGG AGNDIIYGAG GADQLWGGSG SDTFVFAAST DSKPGAADQI MDFVSGLDKI
DLTGITKGAG LHFVNAFTGA AGDAILTTSG GVSTLSVDFS GHGVADFLVS TVGQAAVSDI
VA
//
