ID A0A178MQ06_9PROT Unreviewed; 458 AA.
AC A0A178MQ06;
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=Peptidase {ECO:0000313|EMBL:OAN50902.1};
GN ORFNames=A6A05_11585 {ECO:0000313|EMBL:OAN50902.1};
OS Magnetospirillum moscoviense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1437059 {ECO:0000313|EMBL:OAN50902.1, ECO:0000313|Proteomes:UP000078543};
RN [1] {ECO:0000313|EMBL:OAN50902.1, ECO:0000313|Proteomes:UP000078543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BB-1 {ECO:0000313|EMBL:OAN50902.1,
RC ECO:0000313|Proteomes:UP000078543};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434}.
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:OAN50902.1}.
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DR EMBL; LWQU01000134; OAN50902.1; -; Genomic_DNA.
DR RefSeq; WP_068499871.1; NZ_LWQU01000134.1.
DR AlphaFoldDB; A0A178MQ06; -.
DR STRING; 1437059.A6A05_11585; -.
DR OrthoDB; 9814887at2; -.
DR Proteomes; UP000078543; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000078543};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..458
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008092133"
FT DOMAIN 42..227
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 309..342
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 458 AA; 50243 MW; 2DFBF5D1B150EF12 CRC64;
MLTRIILLSF LVLTLMMPGA AHAQQGQPKR SFIRDAEVEN TIRTFTTPLF QAAGLAPDSV
RLHLMVDPSL NAFVAGGLNM FIHTGLLIRA DSPGQLIGVL AHETGHIAGG HLARIQDAAG
NASTEALIGM LLGAAVGAAT GRADAGAAVM LGSQELAVRN FLTYTRGEES SADQAALRFL
DGTGQSSKGL AEFFEILGDQ ELLVTTRQDP YVRTHPLTRD RISAVRDHVA KSSFSNIPPR
PEWVEMQRRM RGKLFAFIEP PFRTLTRYKD NDASLEARYA RAIALYRKPD MAAALPAIDA
LLAERPKDPY FWELKGQMLF ENGRGTEALA PYAKAVELLP ESALMRIQLA QVQIEQEDPA
LLAEAQKHLA LAVHQEPDNR TGWRLLAIAH GRDGNEGMAA YAMAEQALIE GRLPDASFHA
GKAERLLPKT GEIWLRIQDI KERAAQAADE QKGQRRRR
//
