ID A0A147K5L8_9BACI Unreviewed; 551 AA.
AC A0A147K5L8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=Q75_13845 {ECO:0000313|EMBL:KUP04912.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP04912.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP04912.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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:KUP04912.1}.
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DR EMBL; LDYG01000046; KUP04912.1; -; Genomic_DNA.
DR RefSeq; WP_059283729.1; NZ_LDYG01000046.1.
DR AlphaFoldDB; A0A147K5L8; -.
DR STRING; 1150625.Q75_13845; -.
DR PATRIC; fig|1150625.3.peg.2907; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000074108; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 26..551
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5039761469"
FT DOMAIN 88..138
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 250..396
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 399..550
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 389
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 476
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 551 AA; 60592 MW; F34CA9850FB08414 CRC64;
MKKKKFTTFA VASILSLSLM TPATSAAFLP GVSSQKGIND FELKVKQLDE KGIPSFLSGK
LSNQKIKTEA DVKKFLKDYS SVYQVNTESL KLLDKETDDL GMTHYTFQQT IGNYPIEGAV
FSVHTDKTGS VTVTNGNLYG LKDLAKLKKQ YVHVNGDSAI DLAWKHIDLK PEDTELTETI
ESLHGHDHSL GEEQIKQDTV YIYHEDQFIL AQKVQLQFIE PYGANWQIYV NAVDGSIIKS
KNAIMDAETT GTGTGVNGAS RTLNTYYANG TYYLFDVTKP MNGVIETRTA NYRTSLPGSY
SVDSNNNWSA SSQRAEVDAH YFAGQVYDYY LNKHGRNSYD GNGATIRSTV HYSSNYNNAF
WNGSQMVYGD GDGSTFKALS GSLDVVAHEI THAVTERTAG LVYENQPGAL NESFSDVFGY
FLDTGDYLIG EDVYTPGIAG DALRSMSNPN AYGQPDHMDE YQNLPNTQAG DWGGVHINSG
IPNKAAYYTI QSIGAAKAEK IYYRALTNYL TPYSNFSNAR AAMLQATADL YGSGSSTYSS
VQSAWNSVGV Y
//
