ID A0A178MSK6_9PROT Unreviewed; 463 AA.
AC A0A178MSK6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:OAN52370.1};
GN ORFNames=A6A04_01380 {ECO:0000313|EMBL:OAN52370.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN52370.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN52370.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN52370.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAN52370.1}.
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DR EMBL; LWQT01000044; OAN52370.1; -; Genomic_DNA.
DR RefSeq; WP_068491329.1; NZ_LWQT01000044.1.
DR AlphaFoldDB; A0A178MSK6; -.
DR STRING; 1285242.A6A04_01380; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000078428; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OAN52370.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078428};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..463
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008092231"
FT DOMAIN 38..183
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 192..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 439..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 49979 MW; D84815561FEF01F3 CRC64;
MTLFRLCALF LGLLLAAPSA QARLFDPETF ILANGMQVVV ITNRRAPIVS HMVWYKVGAA
DEVAGKSGLA HLLEHLMFKG TPTVPPGEFS KIVARNGGRD NAFTSSDFTG YYQNVAADKL
ELVMRLESDR MRNLVLDEKN FRTELAVVLE ERRSRVENNP AALLAEQMEA VLYLNSPYQR
PIIGWETEIA GLTLDDALAF YRRWYAPNNA TLIVAGDVDA VTVRPLAEKY YGGIETSVLP
PRARPEEPPI RAPRRISLTD ARVAQPAWIR LYLAPSIRAG QSDLAEPLEV LAEIMGGGST
SRLYRSLVVD RSLAASASVS YDSTAVGQTS LRIGVTPQPG VPLDKLEPLI DQEIAAITKG
AITTDEVERA KARLIASAAY SRDSLHTGAQ TLGQALTVGM TVAEVEAWPE RVAAITPEQV
ARAAALVLDA RGSVTGLLLP DPKAPPGAKP AASPLSGFQK GVH
//
