ID E6XMY6_SHEP2 Unreviewed; 944 AA.
AC E6XMY6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ADV53507.1};
GN OrderedLocusNames=Sput200_1034 {ECO:0000313|EMBL:ADV53507.1};
OS Shewanella putrefaciens (strain 200).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV53507.1, ECO:0000313|Proteomes:UP000008209};
RN [1] {ECO:0000313|EMBL:ADV53507.1, ECO:0000313|Proteomes:UP000008209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200 {ECO:0000313|EMBL:ADV53507.1,
RC ECO:0000313|Proteomes:UP000008209};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA Fredrickson J.K., Woyke T.;
RT "Complete sequence of Shewanella putrefaciens 200.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP002457; ADV53507.1; -; Genomic_DNA.
DR AlphaFoldDB; E6XMY6; -.
DR KEGG; shp:Sput200_1034; -.
DR PATRIC; fig|399804.5.peg.1051; -.
DR HOGENOM; CLU_007487_0_1_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000008209; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..944
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003215518"
FT DOMAIN 58..177
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..390
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 531..662
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 681..856
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 944 AA; 103922 MW; 52C2BDAC1ACD398C CRC64;
MKKWILAVAI SAALSGCAAQ KTTTNLPAGV KLIESVQLAD SQVGIPYKKY QLANGLTVIL
HQDDSDPLVH VDVTYHVGSA RELAGRSGFA HLFEHMMFQG SEHVADEQHF EVVTEAGGTL
NGSTNTDRTN YFETVPSNQL EKMLWLESDR MGFLLPALTS EKFEVQRETV KNERAQRIDN
QPYGRMSERF NQALYPVGHP YSWPVIGWPD DLNRATVDDV KHFFQRWYGP NNATLTIGGD
FDEMQALAWV NKYFGEMPRG PEVSPEPKTS VNLDKTRYIS MEDNVHLPLI RIGFPTVYAR
HQDEAALDLL GNILGGGKTS LVYKNLVKEG HAVQASVSHP CQELACQMSI YALANPEKGG
KLADLEQLIL DSINEFEQRG VTDEDLQKVK VQFEADTIFA LQSVKGKVST LALNQTLFDN
PDLISADLTR YESVTKDDVM RVFKQYIKDK PMVVMSVVPQ GMTALVAHPD NFIPTDLPIA
ETAVEGPLPT AKLVSSFDRT KMPISSAAPM PKVPKIWTTQ LANGIEVMGT QSTETPTVEL
IVYLNGGHRL VPVEKAGLAS LTAEMLNESS QKRSTEALSQ ALEMLGSTVD FSASEYQSTI
KISTLTEHLD ETLAIMEEKL FQPGFTDADF ARVKQQQLQQ IQHMQSNPSY LANSALFSLL
YGKNNALGVS DSGTLDSVAA LTLDDVKAFY AEQYRGANAK IITVANLPES ALLPKLAGLS
RWKGEATSIP ALKPFPELKG GTIYLIDKPG AAQSVINIAK RALPYDATGD YFKAYLMNYP
LGGAFNSRIN LNLRENKGYT YGARTAFSGG AEVGNFVASS DVRTDVTAKA VAEFIKEINA
YQQMGMTDAE LAFMRNSVSQ GQALDYETPY QKAGFMRMIQ RYQLSKDFTA QQDKIINTVT
KDELNSLAAA ELNISQMVIL VVGDKAKIEA DLSTLGYPIE TLVL
//