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Database: UniProt
Entry: A0A143BMA6_9BACT
LinkDB: A0A143BMA6_9BACT
Original site: A0A143BMA6_9BACT 
ID   A0A143BMA6_9BACT        Unreviewed;      1195 AA.
AC   A0A143BMA6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Peptidase M1 membrane alanine aminopeptidase domain-containing protein {ECO:0000259|Pfam:PF01433};
GN   ORFNames=GEMMAAP_14580 {ECO:0000313|EMBL:AMW05695.1};
OS   Gemmatimonas phototrophica.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05695.1, ECO:0000313|Proteomes:UP000076404};
RN   [1] {ECO:0000313|EMBL:AMW05695.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW05695.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA   Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT   "Functional type 2 photosynthetic reaction centers found in the rare
RT   bacterial phylum Gemmatimonadetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN   [2] {ECO:0000313|EMBL:AMW05695.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW05695.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA   Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT   "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT   bacteria in diverse environments.";
RL   Environ. Microbiol. Rep. 8:139-149(2016).
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DR   EMBL; CP011454; AMW05695.1; -; Genomic_DNA.
DR   RefSeq; WP_026848590.1; NZ_CP011454.1.
DR   AlphaFoldDB; A0A143BMA6; -.
DR   STRING; 1379270.GEMMAAP_14580; -.
DR   GeneID; 78445344; -.
DR   KEGG; gph:GEMMAAP_14580; -.
DR   eggNOG; COG0308; Bacteria.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000076404; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF12730; ABC2_membrane_4; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076404};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        106..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        145..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        450..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        474..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        523..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        563..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          866..1071
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   1195 AA;  132715 MW;  1473173B36119C70 CRC64;
     MFGPLFAFEL RGHFRRPTTW LYVAIMFFLA FFALSTEAVL TGAAMGKVKK NSPYALAQMY
     AIMLAIGQII TSALVGSSVL RDFEAGVHEL VFTTRISRSG YLASKYMAAL LAMLLVFAAL
     PLGAIVGSAM PWVDQETLQP INLWFYLQPF LLIGVPGVFF LSALLFSVGS LTRSAFSVYV
     AGILLLVGYS VADELVRTLD RDQLANLIDP FAIRSIDLVT RYWTPVEKNA RTLPVEGFIG
     INRAAWSALG ALLLAVTFRF MRLEKESRVT RKSRASKADA VVRDPVNVLP RAAGSYAPPG
     MVAGWWSVTR FHAQSLVRSV PFLAIATIGL INTLMNAWYA DQNGQNRSWP MSWLMAESSI
     NASFLFMLIL LTFYAGELVW RERQVKLDQV LDASPVQTAS IVLGKMSAML LLLLAFATAA
     MVGTMAVQLL KGYPVLDLPV YGLYVYVADF PTWMPMVALA FLVQALVPRK PIGHVIMILV
     WVSTAATANL GYDYRLLNLL STPSLRWSDL NGTGPYLQAF PAIHGYWTSI GVVLAVLAYL
     SWQRGTADVP FAVRMRARFT GGTRAAVAGG LAGAGAFGGL FFYNASVLNP YFTRKEREQR
     QVRYEQQWRP MERLVLPKVV AVELQVDLAP TAGTARTATS YTVLNRSGVP IDTMLLNVAA
     DAAALTVTLD SVTIDRPFTT IRHDSAWGVH LLRLASPLAP GDSLRVRVVQ RFARRGFPNG
     QPDRSLVENG TFFNREMFPS FGYQASNELA SDELRRKYAL PLARRGKPRT DSAGLQRQSF
     LADADFVTFE ATVSTDPDQI AMAPGYLQKE WTANGRRYFH YVMDTPMPNF FSVLSARWTV
     TKAMWGTVPV EVYHHPTHTF NVARMLDASK ASLAFFSQEF GPYQHRQLRI LEFPRYAGFA
     QSFPNTVPYS EDIGFVARVD SSDVEDTDLP YFVTAHEIAH QWFPYQRMPA DVEGSQMLSE
     SLSEYAALVV TDRQHGRAFT QKFLRAELER YLRGRAGESK GERPLTRVDL QSYIWYQKGA
     IAFFALRDLI GQEALHTALR AYLDEGRFTG PPYATSLDLM RHINAATPDS LKYAIEDYFE
     TITLWDVKTD SLSSTKLANG SYKVVLTATA KKLRADSLGA ETEIPMNDLV DIGVFGAAKT
     GTRIGEALSL RRVRVKAGTA RYEFVVPVKP ARAGIDPYNL LIDRNPGDNS RDIGN
//
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