ID Q5NML3_ZYMMO Unreviewed; 948 AA.
AC Q5NML3;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 2.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:AAV90047.2};
GN OrderedLocusNames=ZMO1423 {ECO:0000313|EMBL:AAV90047.2};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV90047.2, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV90047.2, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; AE008692; AAV90047.2; -; Genomic_DNA.
DR RefSeq; WP_011241205.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NML3; -.
DR SMR; Q5NML3; -.
DR STRING; 264203.ZMO1423; -.
DR KEGG; zmo:ZMO1423; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_007487_0_0_5; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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:SF21; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001173};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..948
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004259847"
FT DOMAIN 60..184
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 218..391
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 674..855
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 462..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 104523 MW; 4FDEDD18133BB5C8 CRC64;
MKKLTRILAC CILSSTLLTP PVIMAHPPIK KAEKTSALLQ SLAKQINLPW QSFTLPNGLR
VLVHTDHKAP VVGVSVWYHV GSKDEPKGKT GFAHLFEHLM FEGSQNIQGS FWKPLRETGA
TDSNGTTNFD RTNYYETVPT SALDRVLYME SDRMGYLLQG MTQEKLDNQR AVVQNEKRQK
DNRPYSAVGY AITQALVPEG HPYHHDTIGS MEDLDAASLD TVKDWFRENY GPNNAVLVLA
GDIDIDKAKT MVNHYFGAIP RGRDIVHPET PIWTLPTRKD EVITDKVALS KIYRAWSIPS
YNNPDSIPLD LSAAVLGGLA SSRLDQILVH QEQLAVNVSA TTQSFEGQGR FLVSVTVKPG
VNPQYVSQRL DKILAEYLEK GATQDEVNRA AMDVLSESVA ESVSAQGPIL AQGLLYAKDP
DYYKKALYAV ATSTAEAVQK STQKWLSRPV YALTVLPGER QAYQESQSGK STPKTDNNLI
LPTAPQPAAS EIASPREALP AVGKVPDVRF PTITHSQLKN GIAVSYAQRP AVPLTTVLIS
FDGGITADTA LPGTESLMLS MLTEGTKEKD VIELSKEKER LGAVISFGAG DDYSSMTFLS
PSVTFRQTTG LASEMLFGST FPEKELARLK ASTLANMAAS RQSPAWLATR ALRQNLYGEG
HPYRHLVTEE NIQKITRQNL LDFRQKWIRP YKAHIFIVSD QSLDQILPVL NNVFGHWQIP
NNAGELKPTS TAKAGHLSDI LLINRPQSPQ SVIMAASVLP LKEKEDQDTL FNLDVANSIL
GGNFLSRLNM DLRQNKGWSY GVGSQINART LSSEFSLAAP VQTNQTAASI NAIQEDINHF
LTDKGITDAE LRETVTGIIN RTPAAYEKSS NILGGMVDLA LMNRPDNYYD TLNQRYRALT
PSELDKTARQ WLSSQALSWV VVGDANLVKP QLEKRGLSVE QVESDKIK
//