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Database: UniProt
Entry: D6E8J1_9ACTN
LinkDB: D6E8J1_9ACTN
Original site: D6E8J1_9ACTN 
ID   D6E8J1_9ACTN            Unreviewed;       932 AA.
AC   D6E8J1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Cell elongation-specific peptidoglycan biosynthesis regulator RodA/cell elongation-specific peptidoglycan D,D-transpeptidase {ECO:0000313|EMBL:CBL04038.1};
GN   ORFNames=GPA_14330 {ECO:0000313|EMBL:CBL04038.1};
OS   Gordonibacter pamelaeae 7-10-1-b.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL04038.1, ECO:0000313|Proteomes:UP000008805};
RN   [1] {ECO:0000313|EMBL:CBL04038.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT   "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL04038.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; FP929047; CBL04038.1; -; Genomic_DNA.
DR   RefSeq; WP_015539388.1; NC_021021.1.
DR   AlphaFoldDB; D6E8J1; -.
DR   KEGG; gpa:GPA_14330; -.
DR   PATRIC; fig|657308.3.peg.1019; -.
DR   HOGENOM; CLU_012814_1_0_11; -.
DR   BioCyc; GPAM657308:GPA_RS06675-MONOMER; -.
DR   Proteomes; UP000008805; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001182; FtsW/RodA.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008805};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        339..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        405..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          609..926
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   932 AA;  98371 MW;  3E7CB0D9B4AEBB82 CRC64;
     MTRRNLELVL LCVAAPIVVL LFAMLAINQG QSLNATTLGV PIGIFVAFVI AHLAVRKFAP
     KADPAILPIS FALSGIGIAF ITRLAPYADK SSIAINQVMW LFLGVACMVL VLVLFRNLDK
     VANYKYTLMI VGFALLLSPL LPVIGQEIYG SRIWIGIPGV FSFQPGEIAK IAIVLFLAGY
     LAQNREMLSV FTWRAGPFNL PDIRTLLPLL LMWLVALLIV VFEKDLGSAL VFFFVFLIML
     YVATGKKFYL VVGLGLIAVG GVGAYLAFGH VQTRVDIWLD PFADAQNTGY QLVQSLYSIA
     DGDLFGVGLG RGLAGGGNGL PQIPVAESDF IFTVIAEEIG LLGAAGVLLL FLCFAIRGFV
     TAARAKSDVS SFVAVGLTSI VVLQAFIIVG GITRLIPLTG ITLPFISQGG SSLLASFIIV
     GFLLRCGDEG TGVGEEMASA TTSLHANSVL GRVSLGKRLT HAMIILSTLF ALLVANLTLI
     MVVQASYYQN MPGNNHTMAK ESRTERGTIS TYDGVILAQS VQQEDGTYER VYPAGNLATH
     VVGYASTQFG TSGIEAAEND TLKGQQNYAS WTDVLNSLAG VGGVGNDVTL TLNSKIQQAA
     QDALSGYAGA CVVMDPETGA VLGMASSPTY DAADFAAEIE KANANPDGES TLLNRAIQTL
     YAPGSTFKIV TLATALEDGV ASEDTVFSSP GTMDIGNAPV TNFNKNSYGD ITLARATELS
     SNTVFGQLGV EMGAEKLVDG ADKFGFNRKI DFTLNTATSL MAEPDEMTKW ELAWSAAGEP
     VNPQNHPSPA GPQATVLEMA LVGCAIANDG AIMNPYLVEG VYNANGERSF TATPNKFLQA
     VSKETASRVK DVLKGVVTDG TGTAAALPGV EVAGKTGTAE KENGNDSWFV GMAPADNPRV
     VVAINLELAD EGMGTERAQN VLRTALQVQG LL
//
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