ID   A0A0N9UR59_SPHMC        Unreviewed;       732 AA.
AC   A0A0N9UR59;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M3 {ECO:0000313|EMBL:ALH78897.1};
GN   ORFNames=AN936_00465 {ECO:0000313|EMBL:ALH78897.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH78897.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH78897.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH78897.1,
RC   ECO:0000313|Proteomes:UP000058074};
RX   PubMed=26634754;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT   Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP012700; ALH78897.1; -; Genomic_DNA.
DR   RefSeq; WP_054586421.1; NZ_CP012700.1.
DR   AlphaFoldDB; A0A0N9UR59; -.
DR   KEGG; smag:AN936_00465; -.
DR   PATRIC; fig|33050.5.peg.92; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000058074; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..732
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006039013"
FT   DOMAIN          276..728
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   732 AA;  81907 MW;  432D3A70C06DFA37 CRC64;
     MPRSAPAVRR RLSTMLASTA MIMGYTIMDI QTASAAQPAP APAAATPAGD NPMLAKWTGP
     FEGVPPWDKM DPELFPDAFQ KAMAETRADV QAVIDNPAEP TFENTHVPMM LAGDTMERLF
     ALWGVQTSNK SNDRVEDIDA EWSPKLTTFY TELFLDPKLF ARYKAVYDKR NSSGLDAQQI
     RIVERSYDEM VRDGANLSAA DKAKLVQMNS KLEGLFSAFS SKLLGDEKLY TFVTDKNELA
     GLEPGFVASL ASAAESQGKP GQWAIKNTRS SAQPVLQGAT NRALRERVYK AFISRGDNGD
     ANDTNATIVE ILKLRQQRAE LLGFPTHAHY RMADTMAKTP EAAMGLMMKV WPAAVARVKE
     EVADMQAIAD AEAKAGNGPK ITIEPWDYRF YSEKVRKAKY DLEESEVKPY LQLDKLRDAM
     FWSAGQLYDL GFRENTGTIP VFDPKVRTFE VYNLKTNENV GVFYLDNFAR DGKRSGAWMT
     TYRSQQTLGG ERNVLASNNN NFTEAAKGEP TLISLDDAQT LFHEFGHGIH YLLQHVTYPA
     LAGVPRDFVE YPSQVNENWL MTPEVLSKYA THYKTGEPMP QALVDKILAS DKFNQGFNTV
     EYLASAIVDM KLHDRKTPPA DVDAFERETL AEMGMPKEIV MRHRLPQFGH LFSSDAYSAG
     YYSYLWSETM DADTWAAFTE AGGPWDRTVA DKFRTILLMT GNETDRAEAY RAFRGRDPDV
     SALLRKRGFP VE
//